CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002952
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chaperone protein HscA 
Protein Synonyms/Alias
 Hsc66 
Gene Name
 hscA 
Gene Synonyms/Alias
 hsc; b2526; JW2510 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
135RVSADILKALAARATacetylation[1]
309ELIAPLVKRTLLACRacetylation[1]
427AQDFTTFKDGQTAMSacetylation[1]
525SYAEQDVKARMLAEQacetylation[1]
590QAIKNVDKQTQDFAAacetylation[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] 
Functional Description
 Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. 
Sequence Annotation
  
Keyword
 3D-structure; ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 616 AA 
Protein Sequence
MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLADHEGR HLLPSVVHYQ 60
QQGHSVGYDA RTNAALDTAN TISSVKRLMG RSLADIQQRY PHLPYQFQAS ENGLPMIETA 120
AGLLNPVRVS ADILKALAAR ATEALAGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL 180
RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD 240
FDHLLADYIR EQAGIPDRSD NRVQRELLDA AIAAKIALSD ADSVTVNVAG WQGEISREQF 300
NELIAPLVKR TLLACRRALK DAGVEADEVL EVVMVGGSTR VPLVRERVGE FFGRPPLTSI 360
DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA 420
QDFTTFKDGQ TAMSIHVMQG ERELVQDCRS LARFALRGIP ALPAGGAHIR VTFQVDADGL 480
LSVTAMEKST GVEASIQVKP SYGLTDSEIA SMIKDSMSYA EQDVKARMLA EQKVEAARVL 540
ESLHGALAAD AALLSAAERQ VIDDAAAHLS EVAQGDDVDA IEQAIKNVDK QTQDFAARRM 600
DQSVRRALKG HSVDEV 616 
Gene Ontology
 GO:0043531; F:ADP binding; IDA:EcoCyc.
 GO:0005524; F:ATP binding; IDA:EcoCyc.
 GO:0016887; F:ATPase activity; IDA:EcoCyc.
 GO:0070417; P:cellular response to cold; IEP:EcoCyc.
 GO:0016226; P:iron-sulfur cluster assembly; IMP:EcoCyc.
 GO:0006457; P:protein folding; IEA:HAMAP. 
Interpro
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam.
 IPR010236; ISC_FeS_clus_asmbl_HscA. 
Pfam
 PF00012; HSP70 
SMART
  
PROSITE
 PS00297; HSP70_1
 PS00329; HSP70_2
 PS01036; HSP70_3 
PRINTS
 PR00301; HEATSHOCK70.