Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP-dependent Clp protease ATP-binding subunit ClpX |
Protein Synonyms/Alias | |
Gene Name | clpX |
Gene Synonyms/Alias | lopC; OrderedLocusNames=b0438, JW0428 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 422 | KPEAQQASGE***** | S | HTP | [1] | |
Reference | [1]Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium. Soares NC,Spät P,Krug K,Macek B J. Proteome Res. 2013, Jun, 7;12(6):2611-21. [ PMID:23590516] |
Functional Description From UniProt | FUNCTION: ATP-dependent specificity component of the Clp protease Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA- sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP |
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| 3D-structure; ATP-binding; Chaperone; Completeproteome; Directproteinsequencing; Host-virusinteraction; Metal-binding; Nucleotide-binding; Referenceproteome; Stressresponse; Zinc; Zinc-finger |
Protein Sequence | 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 424 |
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