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Sequence of CLPX_ECOLI

EC Number:3.4.21.92

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Endopeptidase Clp
P0A6H1
Escherichia coli (strain K12)
424
46356
Reaction
Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec, and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs)
Other sequences found for EC No. 3.4.21.92

General information:

Sequence
show sequence in fasta format
  0 MTDKRKDGSG KLLYCSFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE EIKEVAPHRE
 60 RSALPTPHEI RNHLDDYVIG QEQAKKVLAV AVYNHYKRLR NGDTSNGVEL GKSNILLIGP
120 TGSGKTLLAE TLARLLDVPF TMADATTLTE AGYVGEDVEN IIQKLLQKCD YDVQKAQRGI
180 VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT
240 SKILFICGGA FAGLDKVISH RVETGSGIGF GATVKAKSDK ASEGELLAQV EPEDLIKFGL
300 IPEFIGRLPV VATLNELSEE ALIQILKEPK NALTKQYQAL FNLEGVDLEF RDEALDAIAK
360 KAMARKTGAR GLRSIVEAAL LDTMYDLPSM EDVEKVVIDE SVIDGQSKPL LIYGKPEAQQ
420 ASGE
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1042216
Gottesman S.,Clark W.P.,de Crecy-Lagard V.,Maurizi M.R.
ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities.
J. Biol. Chem.
268
22618-22626
1993
1042217
Yoo S.J.,Seol J.H.,Kang M.S.,Ha D.B.,Chung C.H.
clpX encoding an alternative ATP-binding subunit of protease Ti (Clp) can be expressed independently from clpP in Escherichia coli.
Biochem. Biophys. Res. Commun.
203
798-804
1994
1042219
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
1042220
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
1042221
Wojtkowiak D.,Georgopoulos C.,Zylicz M.
Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.
J. Biol. Chem.
268
22609-22617
1993
1042222
Wawrzynow A.,Wojtkowiak D.,Marszalek J.,Banecki B.,Jonsen M.,Graves B.,Georgopoulos C.,Zylicz M.
The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.
EMBO J.
14
1867-1877
1995
1042223
Kenniston J.A.,Baker T.A.,Fernandez J.M.,Sauer R.T.
Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.
Cell
114
511-520
2003
1042224
Flynn J.M.,Levchenko I.,Sauer R.T.,Baker T.A.
Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation.
Genes Dev.
18
2292-2301
2004
1042225
Chaba R.,Grigorova I.L.,Flynn J.M.,Baker T.A.,Gross C.A.
Design principles of the proteolytic cascade governing the sigmaE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction.
Genes Dev.
21
124-136
2007
1042226
Abdelhakim A.H.,Oakes E.C.,Sauer R.T.,Baker T.A.
Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpX.
Mol. Cell
30
39-50
2008
1042227
Donaldson L.W.,Wojtyra U.,Houry W.A.
Solution structure of the dimeric zinc binding domain of the chaperone ClpX.
J. Biol. Chem.
278
48991-48996
2003
1042228
Park E.Y.,Lee B.G.,Hong S.B.,Kim H.W.,Jeon H.,Song H.K.
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX.
J. Mol. Biol.
367
514-526
2007
1042229
Glynn S.E.,Martin A.,Nager A.R.,Baker T.A.,Sauer R.T.
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
Cell
139
744-756
2009
1042230
Stinson B.M.,Nager A.R.,Glynn S.E.,Schmitz K.R.,Baker T.A.,Sauer R.T.
Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine.
Cell
153
628-639
2013