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Information on EC 7.4.2.9 - ABC-type dipeptide transporter
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7.4.2.9 ABC-type dipeptide transporterIUBMB Comments
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the uptake of di- and tripeptides. The enzyme from Pseudomonas aeruginosa can interact with five different substrate binding proteins.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
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a dipeptide-[dipeptide-binding protein][side 1]
=
+
+
a dipeptide[side 2]
+
[dipeptide-binding protein][side 1]
Synonyms
dppa3, dppa4, dppa2, heme transporter, dipeptide transport system, dppa5, dppabcdf, dppa1, dppbcdf, cellobiose-binding protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ABC-type dipeptide/oligopeptide/nickel transport system
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ABC-type dipeptide/oligopeptide/nickel-transport system
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binding-protein-dependent ABC transporter for dipeptides
dipeptide ABC transporter
dipeptide permease
dipeptide transport system
dipeptide transporting ATPase
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DPP
DppA
dppABCDF
dppB
DppBCDF
dppC
dppD
dppF
TDE_1072
gene name, substrate-binding domain of ABC-type dipeptide/oligopeptide/nickel transport system
TDE_1073
gene name, permease component of ABC-type dipeptide/oligopeptide/nickel transport system
TDE_1074
gene name, permease component of ABC-type dipeptide/oligopeptide/nickel transport system
TDE_1075
gene name, ATPase component of ABC-type dipeptide/oligopeptide/nickel transport system
TDE_1076
gene name, ATPase component of ABC-type dipeptide/oligopeptide/nickel transport system
dipeptide ABC transporter
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DppA
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the gene encodes a periplasmic dipeptide-binding protein required for dipeptide transport and chemotaxis
DppA
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the gene encodes a periplasmic dipeptide-binding protein required for dipeptide transport and chemotaxis
DppA
substrate-binding domain of ABC-type dipeptide/oligopeptide/nickel transport system
DppA
substrate-binding domain of ABC-type dipeptide/oligopeptide/nickel transport system
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dppB
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dppB
permease component of ABC-type dipeptide/oligopeptide/nickel transport system
dppB
permease component of ABC-type dipeptide/oligopeptide/nickel transport system
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dppC
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dppC
permease component of ABC-type dipeptide/oligopeptide/nickel transport system
dppC
permease component of ABC-type dipeptide/oligopeptide/nickel transport system
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dppD
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dppD
ATPase component of ABC-type dipeptide/oligopeptide/nickel transport system
dppD
ATPase component of ABC-type dipeptide/oligopeptide/nickel transport system
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dppF
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dppF
ATPase component of ABC-type dipeptide/oligopeptide/nickel transport system
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1] = ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, dipeptide-transporting)
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the uptake of di- and tripeptides. The enzyme from Pseudomonas aeruginosa can interact with five different substrate binding proteins.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + a tripeptide-[tripeptide-binding protein][side 1]
ADP + phosphate + a tripeptide[side 2] + [tripeptide-binding protein][side 1]
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isoforms DppA2 and DppA4 have a higher tendency to utilize tripeptides as substrate
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-
?
ATP + H2O + delta-aminolevulinic acid-[dipeptide-binding protein DppA][side 1]
ADP + phosphate + delta-aminolevulinic acid[side 2] + [dipeptide-binding protein DppA][side 1]
-
-
-
-
?
ATP + H2O + Gly-Gly-Gly-[tripeptide-binding protein][side 1]
ADP + phosphate + Gly-Gly-Gly[side 2] + [tripeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + Gly-L-His-[dipeptide-binding protein][side 1]
ADP + phosphate + Gly-L-His[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + Gly-L-Leu-[dipeptide-binding protein][side 1]
ADP + phosphate + Gly-L-Leu[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + heme-[dipeptide-binding protein DppA][side 1]
ADP + phosphate + heme[side 2] + [dipeptide-binding protein DppA][side 1]
-
-
-
-
?
ATP + H2O + heme-[L-alanyl-gamma-D-glutamyl-meso-diaminopimelate periplasmic binding protein MppA][side 1]
ADP + phosphate + heme[side 2] + [L-alanyl-gamma-D-glutamyl-meso-diaminopimelate periplasmic binding protein MppA][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-Ala-L-Ala-[ L-Ala-L-Ala-L-Ala-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ala-L-Ala[side 2] + [L-Ala-L-Ala-L-Ala-binding protein][side 1]
ATP + H2O + L-Ala-L-Ala-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ala[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + L-Ala-L-gamma-Glu-L-Leu-[L-Ala-L-gamma-Glu-L-Leu-binding protein][side 1]
ADP + phosphate + L-Ala-L-gamma-Glu-L-Leu[side 2] + [L-Ala-L-gamma-Glu-L-Leu-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-gamma-Glu-L-Phe-L-Leu-[L-Ala-L-gamma-Glu-L-Phe-L-Leu-binding protein][side 1]
ADP + phosphate + L-Ala-L-gamma-Glu-L-Phe-L-Leu[side 2] + [L-Ala-L-gamma-Glu-L-Phe-L-Leu-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-gamma-Glu-O-phospho-L-homoserine-[L-Ala-L-gamma-Glu-O-phospho-L-homoserine-binding protein][side 1]
ADP + phosphate + L-Ala-L-gamma-Glu-O-phospho-L-homoserine[side 2] + [L-Ala-L-gamma-Glu-O-phospho-L-homoserine-binding protein][side 1]
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-
-
-
?
ATP + H2O + L-Ala-L-gamma-Glu-O-phospho-L-serine-[L-Ala-L-gamma-Glu-O-phospho-L-serine-binding protein][side 1]
ADP + phosphate + L-Ala-L-gamma-Glu-O-phospho-L-serine[side 2] + [L-Ala-L-gamma-Glu-O-phospho-L-serine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-Gln-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Ala-L-Gln[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-Ile-[L-Ala-L-Ile-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ile[side 2] + [L-Ala-L-Ile-binding protein][side 1]
ATP + H2O + L-Ala-L-Lys-[L-Ala-L-Lys-binding protein][side 1]
ADP + phosphate + L-Ala-L-Lys[side 2] + [L-Ala-L-Lys-binding protein][side 1]
ATP + H2O + L-Ala-L-Phe-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Ala-L-Phe[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Arg-L-Arg-[L-Arg-L-Arg-binding protein][side 1]
ADP + phosphate + L-Arg-L-Arg[side 2] + [L-Arg-L-Arg-binding protein][side 1]
ATP + H2O + L-Arg-L-Ile-[L-Arg-L-Ile-binding protein][side 1]
ADP + phosphate + L-Arg-L-Ile[side 2] + [L-Arg-L-Ile-binding protein][side 1]
ATP + H2O + L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-[ L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-binding protein][side 1]
ADP + phosphate + L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu[side 2] + [L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-binding protein][side 1]
ATP + H2O + L-His-Gly-[L-His-Gly-binding protein][side 1]
ADP + phosphate + L-His-Gly[side 2] + [L-His-Gly-binding protein][side 1]
ATP + H2O + L-His-L-Ala[dipeptide-binding protein][side 1]
ADP + phosphate + L-His-L-Ala[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + L-Ile-L-Ser-[L-Ile-L-Ser-binding protein][side 1]
ADP + phosphate + L-Ile-L-Ser[side 2] + [L-Ile-L-Ser-binding protein][side 1]
ATP + H2O + L-Ile-L-Trp-L-Val-L-Asn-[L-Ile-L-Trp-L-Val-L-Asn-binding protein][side 1]
ADP + phosphate + L-Ile-L-Trp-L-Val-L-Asn[side 2] + [L-Ile-L-Trp-L-Val-L-Asn-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Leu-Gly-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Leu-Gly[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + L-Leu-L-Leu-L-Leu-[L-Leu-L-Leu-L-Leu-binding protein][side 1]
ADP + phosphate + L-Leu-L-Leu-L-Leu[side 2] + [L-Leu-L-Leu-L-Leu-binding protein][side 1]
ATP + H2O + L-Leu-L-Leu-[L-Leu-L-Leu-binding protein][side 1]
ADP + phosphate + L-Leu-L-Leu[side 2] + [L-Leu-L-Leu-binding protein][side 1]
-
high-affinity substrate
-
-
?
ATP + H2O + L-Leu-L-Val-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Leu-L-Val[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + L-Lys-L-Ile-[L-Lys-L-Ile-binding protein][side 1]
ADP + phosphate + L-Lys-L-Ile[side 2] + [L-Lys-L-Ile-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Phe-L-Ile-[L-Phe-L-Ile-binding protein][side 1]
ADP + phosphate + L-Phe-L-Ile[side 2] + [L-Phe-L-Ile-binding protein][side 1]
-
-
-
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?
ATP + H2O + L-Phe-L-Pro-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Phe-L-Pro[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Phe-L-Val-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Phe-L-Val[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Pro-Gly-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Pro-Gly[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + L-Pro-L-Leu-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Pro-L-Leu[side 2] + [dipeptide-binding protein][side 1]
-
-
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?
ATP + H2O + L-Pro-L-Phe-L-Lys-[tripeptide-binding protein][side 1]
ADP + phosphate + L-Pro-L-Phe-L-Lys[side 2] + [tripeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Pro-L-Val-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Pro-L-Val[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + L-Thr-L-Gln-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Thr-L-Gln[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Val-L-Ile-[L-Val-L-Ile-binding protein][side 1]
ADP + phosphate + L-Val-L-Ile[side 2] + [L-Val-L-Ile-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Val-L-Trp-L-Ile-[L-Val-L-Trp-L-Ile-binding protein][side 1]
ADP + phosphate + L-Val-L-Trp-L-Ile[side 2] + [L-Val-L-Trp-L-Ile-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-[L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-binding protein][side 1]
ADP + phosphate + L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe[side 2] + [L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Val-L-Val-L-Val-[L-Val-L-Val-L-Val-binding protein][side 1]
ADP + phosphate + L-Val-L-Val-L-Val[side 2] + [L-Val-L-Val-L-Val-binding protein][side 1]
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high-affinity substrate
-
-
?
ATP + H2O + L-Val-L-Val-[L-Val-L-Val-binding protein][side 1]
ADP + phosphate + L-Val-L-Val[side 2] + [L-Val-L-Val-binding protein][side 1]
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high-affinity substrate
-
-
?
ATP + H2O + phaseolotoxin-[tripeptide-binding protein][side 1]
ADP + phosphate + phaseolotoxin[side 2] + [tripeptide-binding protein][side 1]
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-
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?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
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?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
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-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
Lactococcus cremoris MG1363
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-
-
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?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
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-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
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-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
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-
-
?
ATP + H2O + Gly-L-His-[dipeptide-binding protein][side 1]
ADP + phosphate + Gly-L-His[side 2] + [dipeptide-binding protein][side 1]
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-
-
-
?
ATP + H2O + Gly-L-His-[dipeptide-binding protein][side 1]
ADP + phosphate + Gly-L-His[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + Gly-L-Leu-[dipeptide-binding protein][side 1]
ADP + phosphate + Gly-L-Leu[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + Gly-L-Leu-[dipeptide-binding protein][side 1]
ADP + phosphate + Gly-L-Leu[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-Ala-L-Ala-[ L-Ala-L-Ala-L-Ala-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ala-L-Ala[side 2] + [L-Ala-L-Ala-L-Ala-binding protein][side 1]
-
high-affinity substrate
-
-
?
ATP + H2O + L-Ala-L-Ala-L-Ala-[ L-Ala-L-Ala-L-Ala-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ala-L-Ala[side 2] + [L-Ala-L-Ala-L-Ala-binding protein][side 1]
Lactococcus cremoris MG1363
-
high-affinity substrate
-
-
?
ATP + H2O + L-Ala-L-Ala-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ala[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-Ala-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ala[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-Ile-[L-Ala-L-Ile-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ile[side 2] + [L-Ala-L-Ile-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-Ile-[L-Ala-L-Ile-binding protein][side 1]
ADP + phosphate + L-Ala-L-Ile[side 2] + [L-Ala-L-Ile-binding protein][side 1]
Helicobacter pylori 43504
-
-
-
-
?
ATP + H2O + L-Ala-L-Lys-[L-Ala-L-Lys-binding protein][side 1]
ADP + phosphate + L-Ala-L-Lys[side 2] + [L-Ala-L-Lys-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ala-L-Lys-[L-Ala-L-Lys-binding protein][side 1]
ADP + phosphate + L-Ala-L-Lys[side 2] + [L-Ala-L-Lys-binding protein][side 1]
Helicobacter pylori 43504
-
-
-
-
?
ATP + H2O + L-Arg-L-Arg-[L-Arg-L-Arg-binding protein][side 1]
ADP + phosphate + L-Arg-L-Arg[side 2] + [L-Arg-L-Arg-binding protein][side 1]
-
high-affinity substrate
-
-
?
ATP + H2O + L-Arg-L-Arg-[L-Arg-L-Arg-binding protein][side 1]
ADP + phosphate + L-Arg-L-Arg[side 2] + [L-Arg-L-Arg-binding protein][side 1]
Lactococcus cremoris MG1363
-
high-affinity substrate
-
-
?
ATP + H2O + L-Arg-L-Ile-[L-Arg-L-Ile-binding protein][side 1]
ADP + phosphate + L-Arg-L-Ile[side 2] + [L-Arg-L-Ile-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Arg-L-Ile-[L-Arg-L-Ile-binding protein][side 1]
ADP + phosphate + L-Arg-L-Ile[side 2] + [L-Arg-L-Ile-binding protein][side 1]
Helicobacter pylori 43504
-
-
-
-
?
ATP + H2O + L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-[ L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-binding protein][side 1]
ADP + phosphate + L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu[side 2] + [L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-[ L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-binding protein][side 1]
ADP + phosphate + L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu[side 2] + [L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu-binding protein][side 1]
Helicobacter pylori 43504
-
-
-
-
?
ATP + H2O + L-His-Gly-[L-His-Gly-binding protein][side 1]
ADP + phosphate + L-His-Gly[side 2] + [L-His-Gly-binding protein][side 1]
-
low-affinity substrate
-
-
?
ATP + H2O + L-His-Gly-[L-His-Gly-binding protein][side 1]
ADP + phosphate + L-His-Gly[side 2] + [L-His-Gly-binding protein][side 1]
Lactococcus cremoris MG1363
-
low-affinity substrate
-
-
?
ATP + H2O + L-His-L-Ala[dipeptide-binding protein][side 1]
ADP + phosphate + L-His-L-Ala[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-His-L-Ala[dipeptide-binding protein][side 1]
ADP + phosphate + L-His-L-Ala[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ile-L-Ser-[L-Ile-L-Ser-binding protein][side 1]
ADP + phosphate + L-Ile-L-Ser[side 2] + [L-Ile-L-Ser-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Ile-L-Ser-[L-Ile-L-Ser-binding protein][side 1]
ADP + phosphate + L-Ile-L-Ser[side 2] + [L-Ile-L-Ser-binding protein][side 1]
Helicobacter pylori 43504
-
-
-
-
?
ATP + H2O + L-Leu-Gly-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Leu-Gly[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Leu-Gly-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Leu-Gly[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Leu-L-Leu-L-Leu-[L-Leu-L-Leu-L-Leu-binding protein][side 1]
ADP + phosphate + L-Leu-L-Leu-L-Leu[side 2] + [L-Leu-L-Leu-L-Leu-binding protein][side 1]
-
high-affinity substrate
-
-
?
ATP + H2O + L-Leu-L-Leu-L-Leu-[L-Leu-L-Leu-L-Leu-binding protein][side 1]
ADP + phosphate + L-Leu-L-Leu-L-Leu[side 2] + [L-Leu-L-Leu-L-Leu-binding protein][side 1]
Lactococcus cremoris MG1363
-
high-affinity substrate
-
-
?
ATP + H2O + L-Leu-L-Val-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Leu-L-Val[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Leu-L-Val-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Leu-L-Val[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Pro-Gly-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Pro-Gly[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Pro-Gly-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Pro-Gly[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Pro-Gly-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Pro-Gly[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Pro-L-Val-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Pro-L-Val[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-Pro-L-Val-[dipeptide-binding protein][side 1]
ADP + phosphate + L-Pro-L-Val[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
additional information
?
-
-
dipeptides containing uncharged residues, either at the N- or C-terminal end, are better substrates than nonpolar and acidic ones
-
-
?
additional information
?
-
-
the enzyme also functions as maltose and cellobiose transporter
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
ATP + H2O + a tripeptide-[tripeptide-binding protein][side 1]
ADP + phosphate + a tripeptide[side 2] + [tripeptide-binding protein][side 1]
-
isoforms DppA2 and DppA4 have a higher tendency to utilize tripeptides as substrate
-
-
?
ATP + H2O + delta-aminolevulinic acid-[dipeptide-binding protein DppA][side 1]
ADP + phosphate + delta-aminolevulinic acid[side 2] + [dipeptide-binding protein DppA][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
Lactococcus cremoris MG1363
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
?
ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1]
ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Aberrant expression of DPPA2 and HIWI genes in colorectal cancer and their impacts on poor prognosis.
Carcinogenesis
Ectopic Expression of Human DPPA2 Gene in ESCC Cell Line Using Retroviral System.
Carcinoma
Ectopic Expression of Human DPPA2 Gene in ESCC Cell Line Using Retroviral System.
Carcinoma
Identification of DPPA4 and DPPA2 as a novel family of pluripotency-related oncogenes.
Carcinoma
The expressions of stem cell markers: Oct4, Nanog, Sox2, nucleostemin, Bmi, Zfx, Tcl1, Tbx3, Dppa4, and Esrrb in bladder, colon, and prostate cancer, and certain cancer cell lines.
Carcinoma, Embryonal
Differentiation of human embryonal carcinomas in vitro and in vivo reveals expression profiles relevant to normal development.
Carcinoma, Embryonal
Dppa2 and Dppa4 are closely linked SAP motif genes restricted to pluripotent cells and the germ line.
Carcinoma, Embryonal
Genomic functions of developmental pluripotency associated factor 4 (Dppa4) in pluripotent stem cells and cancer.
Carcinoma, Embryonal
Identification of DPPA4 and DPPA2 as a novel family of pluripotency-related oncogenes.
Carcinoma, Embryonal
The role of promoter CpG methylation in the epigenetic control of stem cell related genes during differentiation.
Carcinoma, Hepatocellular
PGC7 promotes tumor oncogenic dedifferentiation through remodeling DNA methylation pattern for key developmental transcription factors.
Colonic Neoplasms
Developmental pluripotency-associated 4: a novel predictor for prognosis and a potential therapeutic target for colon cancer.
Colorectal Neoplasms
Aberrant expression of DPPA2 and HIWI genes in colorectal cancer and their impacts on poor prognosis.
Colorectal Neoplasms
Developmental pluripotency-associated 4: a novel predictor for prognosis and a potential therapeutic target for colon cancer.
Endodermal Sinus Tumor
Gene expression profiling differentiates germ cell tumors from other cancers and defines subtype-specific signatures.
Endometriosis
Expression Pattern of Stemness-Related Genes in Human Endometrial and Endometriotic Tissues.
Esophageal Squamous Cell Carcinoma
Ectopic Expression of Human DPPA2 Gene in ESCC Cell Line Using Retroviral System.
Infections
A Novel Heme Transporter from the Energy Coupling Factor Family Is Vital for Group A Streptococcus Colonization and Infections.
Infections
Active and passive immunizations with HtsA, a streptococcal heme transporter protein, protect mice from subcutaneous group A Streptococcus infection.
Infections
The Heme Transporter HtsABC of Group A Streptococcus Contributes to Virulence and Innate Immune Evasion in Murine Skin Infections.
Leukemia, Feline
Placental expression of the heme transporter, feline leukemia virus subgroup C receptor, is related to maternal iron status in pregnant adolescents.
Lung Neoplasms
High developmental pluripotency?associated 4 expression promotes cell proliferation and glycolysis, and predicts poor prognosis in non?small?cell lung cancer.
Lymphatic Metastasis
Aberrant expression of DPPA2 and HIWI genes in colorectal cancer and their impacts on poor prognosis.
Lymphatic Metastasis
DPPA2 Protein Expression is Associated with Gastric Cancer Metastasis.
Melanoma
Transcriptome analysis during human trophectoderm specification suggests new roles of metabolic and epigenetic genes.
Neoplasm Metastasis
Aberrant expression of DPPA2 and HIWI genes in colorectal cancer and their impacts on poor prognosis.
Neoplasm Metastasis
Developmental pluripotency-associated 4: a novel predictor for prognosis and a potential therapeutic target for colon cancer.
Neoplasms
Aberrant expression of DPPA2 and HIWI genes in colorectal cancer and their impacts on poor prognosis.
Neoplasms
Carrier-mediated transport of oligopeptides in the human fibrosarcoma cell line HT1080.
Neoplasms
Developmental pluripotency-associated 4: a novel predictor for prognosis and a potential therapeutic target for colon cancer.
Neoplasms
Dppa3 is a marker of pluripotency and has a human homologue that is expressed in germ cell tumours.
Neoplasms
Ectopic Expression of Human DPPA2 Gene in ESCC Cell Line Using Retroviral System.
Neoplasms
Expression and serum immunoreactivity of developmentally restricted differentiation antigens in epithelial ovarian cancer.
Neoplasms
Gene expression profiling differentiates germ cell tumors from other cancers and defines subtype-specific signatures.
Neoplasms
High developmental pluripotency?associated 4 expression promotes cell proliferation and glycolysis, and predicts poor prognosis in non?small?cell lung cancer.
Neoplasms
Identification of DPPA4 and DPPA2 as a novel family of pluripotency-related oncogenes.
Neoplasms
Imprints and DPPA3 are bypassed during pluripotency- and differentiation-coupled methylation reprogramming in testicular germ cell tumors.
Neoplasms
PGC7 promotes tumor oncogenic dedifferentiation through remodeling DNA methylation pattern for key developmental transcription factors.
Neoplasms
SPOP suppresses testicular germ cell tumors progression through ubiquitination and degradation of DPPA2.
Neoplasms
The expressions of stem cell markers: Oct4, Nanog, Sox2, nucleostemin, Bmi, Zfx, Tcl1, Tbx3, Dppa4, and Esrrb in bladder, colon, and prostate cancer, and certain cancer cell lines.
Neoplasms
The role of promoter CpG methylation in the epigenetic control of stem cell related genes during differentiation.
Neoplasms, Germ Cell and Embryonal
Dppa3 is a marker of pluripotency and has a human homologue that is expressed in germ cell tumours.
Neoplasms, Germ Cell and Embryonal
Identification of DPPA4 and DPPA2 as a novel family of pluripotency-related oncogenes.
Neoplasms, Germ Cell and Embryonal
Imprints and DPPA3 are bypassed during pluripotency- and differentiation-coupled methylation reprogramming in testicular germ cell tumors.
Neoplasms, Germ Cell and Embryonal
SPOP suppresses testicular germ cell tumors progression through ubiquitination and degradation of DPPA2.
Obesity
Embryonic defects induced by maternal obesity in mice derive from Stella insufficiency in oocytes.
Persistent Infection
Brucella abortus Requires the Heme Transporter BhuA for Maintenance of Chronic Infection in BALB/c Mice.
Prostatic Neoplasms
The expressions of stem cell markers: Oct4, Nanog, Sox2, nucleostemin, Bmi, Zfx, Tcl1, Tbx3, Dppa4, and Esrrb in bladder, colon, and prostate cancer, and certain cancer cell lines.
Seminoma
Gene expression profiling differentiates germ cell tumors from other cancers and defines subtype-specific signatures.
Squamous Cell Carcinoma of Head and Neck
Copy number increase of oncoprotein CIP2A is associated with poor patient survival in human head and neck squamous cell carcinoma.
Teratoma
Gene expression profiling differentiates germ cell tumors from other cancers and defines subtype-specific signatures.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1451
L-Ala-L-gamma-Glu-L-Leu-[L-Ala-L-gamma-Glu-L-Leu-binding protein][side 1]
-
at pH 7.0 and 37°C
-
1.335
L-Ala-L-gamma-Glu-L-Phe-L-Leu-[L-Ala-L-gamma-Glu-L-Phe-L-Leu-binding protein][side 1]
-
at pH 7.0 and 37°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24.4
L-Ala-L-gamma-Glu-L-Leu-[L-Ala-L-gamma-Glu-L-Leu-binding protein][side 1]
-
at pH 7.0 and 37°C
-
8.31
L-Ala-L-gamma-Glu-L-Phe-L-Leu-[L-Ala-L-gamma-Glu-L-Phe-L-Leu-binding protein][side 1]
-
at pH 7.0 and 37°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
168
L-Ala-L-gamma-Glu-L-Leu-[L-Ala-L-gamma-Glu-L-Leu-binding protein][side 1]
-
at pH 7.0 and 37°C
-
6.22
L-Ala-L-gamma-Glu-L-Phe-L-Leu-[L-Ala-L-gamma-Glu-L-Phe-L-Leu-binding protein][side 1]
-
at pH 7.0 and 37°C
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
serotype M49 group A
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is responsible for the initial binding of peptides in the periplasmic space
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DPPD_CALS4
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
326
0
36361
Swiss-Prot
-
DPPD_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
330
0
36328
Swiss-Prot
-
DPPD_LACLM
Lactococcus lactis subsp. cremoris (strain MG1363)
349
0
38910
Swiss-Prot
-
DPPD_PSEAB
Pseudomonas aeruginosa (strain UCBPP-PA14)
324
0
35399
Swiss-Prot
-
DPPF_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
327
0
36917
Swiss-Prot
-
DPPF_LACLM
Lactococcus lactis subsp. cremoris (strain MG1363)
312
0
34883
Swiss-Prot
-
DPPF_PSEAB
Pseudomonas aeruginosa (strain UCBPP-PA14)
323
0
36363
Swiss-Prot
-
Q73NS6_TREDE
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
346
0
39139
TrEMBL
-
Q73NS7_TREDE
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
325
0
36460
TrEMBL
-
Q73NS8_TREDE
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
464
0
51598
TrEMBL
-
Q73NS9_TREDE
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
346
0
39096
TrEMBL
-
Q73NT0_TREDE
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
871
0
95556
TrEMBL
-
Q9ZAS3_STRPY
267
0
29396
TrEMBL
other Location (Reliability: 1)
Q9ZAS4_STRPY
274
0
30567
TrEMBL
Secretory Pathway (Reliability: 2)
Q9ZAS5_STRPY
325
0
36141
TrEMBL
other Location (Reliability: 4)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nucleotide-binding domain DppD bound with ATP, Mg2+ and a [4Fe-4S] cluster, hanging drop vapor diffusion method, using 4% (v/v) 2-propanol, 0.05 M CAPSO pH 11.0, 12.25% (w/v) polyethylene glycol monomethyl ether 5000
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni Sepharose 6 column chromatography and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C43 (DE3) cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
DppA expression is repressed by tri-leucine and tri-valine
expression of the dpp operon is induced approximately 4fold in late exponential growth phase. Enzyme expression is decreased about 4fold in a Mga virulence regulator mutant
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, X.; Zhuo, W.; Yu, J.; Ge, J.; Gu, J.; Feng, Y.; Yang, M.; Wang, L.; Wang, N.
Structure of the nucleotide-binding domain of a dipeptide ABC transporter reveals a novel iron-sulfur cluster-binding domain
Acta Crystallogr. Sect. D
69
256-265
2013
Caldanaerobacter subterraneus subsp. tengcongensis
brenda
Kuenzl, T.; Li-Blatter, X.; Srivastava, P.; Herdewijn, P.; Sharpe, T.; Panke, S.
Mutant variants of the substrate-binding protein DppA from Escherichia coli enhance growth on nonstandard gamma-glutamyl amide-containing peptides
Appl. Environ. Microbiol.
84
e00340-18
2018
Escherichia coli
brenda
Sanz, Y.; Lanfermeijer, F.C.; Renault, P.; Bolotin, A.; Konings, W.N.; Poolman, B.
Genetic and functional characterization of dpp genes encoding a dipeptide transport system in Lactococcus lactis
Arch. Microbiol.
175
334-343
2001
Lactococcus cremoris, Lactococcus cremoris MG1363
brenda
Weinberg, M.V.; Maier, R.J.
Peptide transport in Helicobacter pylori roles of Dpp and Opp systems and evidence for additional peptide transporters
J. Bacteriol.
189
3392-3402
2007
Helicobacter pylori, Helicobacter pylori 43504
brenda
Asai, T.; Okamoto-Shibayama, K.; Kikuchi, Y.; Ishihara, K.
Characterization of a novel potential peptide import system in Treponema denticola
Microb. Pathog.
123
467-472
2018
Treponema denticola (Q73NS6), Treponema denticola (Q73NS7), Treponema denticola (Q73NS8), Treponema denticola (Q73NS9), Treponema denticola (Q73NT0), Treponema denticola, Treponema denticola ATCC 35405 (Q73NS6), Treponema denticola ATCC 35405 (Q73NS7), Treponema denticola ATCC 35405 (Q73NS8), Treponema denticola ATCC 35405 (Q73NS9), Treponema denticola ATCC 35405 (Q73NT0)
brenda
Podbielski, A.; Leonard, B.A.
The group A streptococcal dipeptide permease (Dpp) is involved in the uptake of essential amino acids and affects the expression of cysteine protease
Mol. Microbiol.
28
1323-1334
1998
Streptococcus pyogenes (Q9ZAS2), Streptococcus pyogenes (Q9ZAS3), Streptococcus pyogenes (Q9ZAS4), Streptococcus pyogenes (Q9ZAS5), Streptococcus pyogenes (Q9ZAS6)
brenda
Elferink, M.G.; Albers, S.V.; Konings, W.N.; Driessen, A.J.
Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters
Mol. Microbiol.
39
1494-1503
2001
Saccharolobus solfataricus
brenda
Abouhamad, W.; Manson, M.; Gibson, M.; Higgins, C.
Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein
Mol. Microbiol.
5
1035-1047
1991
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Pletzer, D.; Lafon, C.; Braun, Y.; Koehler, T.; Page, M.G.; Mourez, M.; Weingart, H.
High-throughput screening of dipeptide utilization mediated by the ABC transporter DppBCDF and its substrate-binding proteins DppA1-A5 in Pseudomonas aeruginosa
PLoS ONE
9
e111311
2014
Pseudomonas aeruginosa
brenda
Letoffe, S.; Delepelaire, P.; Wandersman, C.
The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins
Proc. Natl. Acad. Sci. USA
103
12891-12896
2006
Escherichia coli
brenda
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EXTERNAL LINKS (specific for EC-Number 7.4.2.9)
Transporter Classification Database (TCDB): 3.A.1.5.2, 3.A.1.5.27
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Release 2023.1 (January 2023)
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