CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002953
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chaperone protein HtpG 
Protein Synonyms/Alias
 Heat shock protein C62.5; Heat shock protein HtpG; High temperature protein G 
Gene Name
 htpG 
Gene Synonyms/Alias
 b0473; JW0462 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
45NASDAADKLRFRALSacetylation[1]
71RVRVSFDKDKRTLTIacetylation[1]
147RTRAAGEKPENGVFWacetylation[1]
199RVRSIISKYSDHIALacetylation[1]
212ALPVEIEKREEKDGEacetylation[1]
216EIEKREEKDGETVISacetylation[1]
226ETVISWEKINKAQALacetylation[1]
229ISWEKINKAQALWTRacetylation[1, 2]
238QALWTRNKSEITDEEacetylation[1, 2]
247EITDEEYKEFYKHIAacetylation[1]
251EEYKEFYKHIAHDFNacetylation[1]
271SHNRVEGKQEYTSLLacetylation[1]
294DMWNRDHKHGLKLYVacetylation[1]
298RDHKHGLKLYVQRVFacetylation[1]
362RVLQMLEKLAKDDAEacetylation[1, 3]
365QMLEKLAKDDAEKYQacetylation[1]
370LAKDDAEKYQTFWQQacetylation[1]
398ANQEAIAKLLRFASTacetylation[1]
429RMKEGQEKIYYITADacetylation[1]
442ADSYAAAKSSPHLELacetylation[1]
485KPFQSVSKVDESLEKacetylation[1]
492KVDESLEKLADEVDEacetylation[1]
502DEVDESAKEAEKALTacetylation[1]
506ESAKEAEKALTPFIDacetylation[1]
552EMSTQMAKLFAAAGQacetylation[1]
560LFAAAGQKVPEVKYIacetylation[1]
565GQKVPEVKYIFELNPacetylation[1]
578NPDHVLVKRAADTEDacetylation[1]
Reference
 [1] 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]
 [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] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 
Functional Description
 Molecular chaperone. Has ATPase activity. 
Sequence Annotation
 REGION 1 336 A; substrate-binding.
 REGION 337 552 B.
 REGION 553 624 C.
 REGION 585 624 Mediates dimerization.
 BINDING 38 38 ATP.
 BINDING 80 80 ATP.
 BINDING 127 127 ATP; via amide nitrogen.
 BINDING 174 174 ATP.
 BINDING 255 255 ATP.  
Keyword
 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 624 AA 
Protein Sequence
MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD 60
GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS GTKSFLESLG SDQAKDSQLI 120
GQFGVGFYSA FIVADKVTVR TRAAGEKPEN GVFWESAGEG EYTVADITKE DRGTEITLHL 180
REGEDEFLDD WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE 240
ITDEEYKEFY KHIAHDFNDP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY 300
VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN ALTKRVLQML 360
EKLAKDDAEK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL RFASTHTDSS AQTVSLEDYV 420
SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF 480
QSVSKVDESL EKLADEVDES AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS 540
TDADEMSTQM AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA 600
LLAERGTLED PNLFIRRMNQ LLVS 624 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0042623; F:ATPase activity, coupled; IDA:EcoCyc.
 GO:0006457; P:protein folding; EXP:EcoCyc.
 GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki.
 GO:0009408; P:response to heat; IEP:EcoliWiki. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR019805; Heat_shock_protein_90_CS.
 IPR001404; Hsp90.
 IPR020575; Hsp90_N.
 IPR020568; Ribosomal_S5_D2-typ_fold. 
Pfam
 PF02518; HATPase_c
 PF00183; HSP90 
SMART
 SM00387; HATPase_c 
PROSITE
 PS00298; HSP90 
PRINTS
 PR00775; HEATSHOCK90.