CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009736
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chaperone protein ClpB 
Protein Synonyms/Alias
 Heat shock protein F84.1 
Gene Name
 clpB 
Gene Synonyms/Alias
 htpM; b2592; JW2573 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
96RVLNLCDKLAQKRGDacetylation[1, 2, 3]
100LCDKLAQKRGDNFISacetylation[3]
127GTLADILKAAGATTAacetylation[2]
162EDQRQALKKYTIDLTacetylation[3]
163DQRQALKKYTIDLTEacetylation[2, 3]
176TERAEQGKLDPVIGRacetylation[1, 3]
233GEVPEGLKGRRVLALacetylation[3]
250GALVAGAKYRGEFEEacetylation[3]
300MDAGNMLKPALARGEacetylation[3]
325EYRQYIEKDAALERRacetylation[3]
335ALERRFQKVFVAEPSacetylation[3]
389ADRQLPDKAIDLIDEacetylation[3]
408IRMQIDSKPEELDRLacetylation[3]
423DRRIIQLKLEQQALMacetylation[3]
431LEQQALMKESDEASKacetylation[3]
439ESDEASKKRLDMLNEacetylation[3]
451LNEELSDKERQYSELacetylation[3]
463SELEEEWKAEKASLSacetylation[3]
476LSGTQTIKAELEQAKacetylation[3]
483KAELEQAKIAIEQARacetylation[3]
505MSELQYGKIPELEKQacetylation[3]
511GKIPELEKQLEAATQacetylation[3]
522AATQLEGKTMRLLRNacetylation[3]
530TMRLLRNKVTDAEIAacetylation[2, 3]
558MMESEREKLLRMEQEacetylation[3]
611LGPTGVGKTELCKALacetylation[3]
616VGKTELCKALANFMFacetylation[3]
640DMSEFMEKHSVSRLVacetylation[1, 2, 3]
738ELDYAHMKELVLGVVacetylation[3]
780SIAQIQLKRLYKRLEacetylation[3]
801HISDEALKLLSENGYacetylation[3]
818VYGARPLKRAIQQQIacetylation[3]
842SGELVPGKVIRLEVNacetylation[2, 3]
Reference
 [1] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [3] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. 
Sequence Annotation
 NP_BIND 206 213 ATP 1.
 NP_BIND 605 612 ATP 2.
 REGION 1 143 N-terminal.
 REGION 159 340 NBD1.
 REGION 341 545 Linker.
 REGION 555 765 NBD2.
 REGION 766 857 C-terminal.
 MOD_RES 96 96 N6-acetyllysine.
 MOD_RES 176 176 N6-acetyllysine.
 MOD_RES 640 640 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative initiation; ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Reference proteome; Repeat; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 857 AA 
Protein Sequence
MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL TSAGINAGQL 60
RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK RGDNFISSEL FVLAALESRG 120
TLADILKAAG ATTANITQAI EQMRGGESVN DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV 180
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL 240
DMGALVAGAK YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK 300
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL RGLKERYELH 360
HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE ELDRLDRRII 420
QLKLEQQALM KESDEASKKR LDMLNEELSD KERQYSELEE EWKAEKASLS GTQTIKAELE 480
QAKIAIEQAR RVGDLARMSE LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL 540
ARWTGIPVSR MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS 600
FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG 660
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL 720
GSDLIQERFG ELDYAHMKEL VLGVVSHNFR PEFINRIDEV VVFHPLGEQH IASIAQIQLK 780
RLYKRLEERG YEIHISDEAL KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP 840
GKVIRLEVNE DRIVAVQ 857 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0016485; P:protein processing; IEA:InterPro.
 GO:0009408; P:response to heat; IEA:InterPro.
 GO:0006986; P:response to unfolded protein; IDA:EcoCyc. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR013093; ATPase_AAA-2.
 IPR003959; ATPase_AAA_core.
 IPR018368; Chaperonin_ClpA/B_CS.
 IPR017730; Chaperonin_ClpB.
 IPR001270; Chaprnin_ClpA/B.
 IPR019489; Clp_ATPase_C.
 IPR004176; Clp_N.
 IPR023150; Dbl_Clp-N.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA
 PF07724; AAA_2
 PF02861; Clp_N
 PF10431; ClpB_D2-small 
SMART
 SM00382; AAA
 SM01086; ClpB_D2-small 
PROSITE
 PS00870; CLPAB_1
 PS00871; CLPAB_2 
PRINTS
 PR00300; CLPPROTEASEA.