CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002906
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60 kDa chaperonin 
Protein Synonyms/Alias
 GroEL protein; Protein Cpn60 
Gene Name
 groL 
Gene Synonyms/Alias
 groEL; mopA; b4143; JW4103 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
7*MAAKDVKFGNDARVacetylation[1]
28NVLADAVKVTLGPKGacetylation[1]
42GRNVVLDKSFGAPTIacetylation[1, 2, 3]
51FGAPTITKDGVSVARacetylation[1, 3]
65REIELEDKFENMGAQacetylation[1]
65REIELEDKFENMGAQpupylation[4]
80MVKEVASKANDAAGDacetylation[1]
105AIITEGLKAVAAGMNacetylation[1, 3]
117GMNPMDLKRGIDKAVacetylation[1, 3, 5]
122DLKRGIDKAVTAAVEacetylation[1, 2, 3]
132TAAVEELKALSVPCSacetylation[1, 3]
142SVPCSDSKAIAQVGTacetylation[1, 3]
160NSDETVGKLIAEAMDacetylation[1, 3]
168LIAEAMDKVGKEGVIacetylation[1, 3]
168LIAEAMDKVGKEGVIpupylation[4]
207LSPYFINKPETGAVEacetylation[1, 3]
225PFILLADKKISNIREacetylation[1]
226FILLADKKISNIREMacetylation[3]
242PVLEAVAKAGKPLLIacetylation[1, 3]
272NTMRGIVKVAAVKAPacetylation[1, 3]
277IVKVAAVKAPGFGDRacetylation[1, 3]
321LEDLGQAKRVVINKDacetylation[1, 3]
321LEDLGQAKRVVINKDpupylation[4]
327AKRVVINKDTTTIIDacetylation[1, 3]
364TSDYDREKLQERVAKacetylation[1, 3]
371KLQERVAKLAGGVAVacetylation[1]
390AATEVEMKEKKARVEacetylation[1]
425ALIRVASKLADLRGQacetylation[1, 2, 3]
441EDQNVGIKVALRAMEacetylation[1, 3]
498MGILDPTKVTRSALQacetylation[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] 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]
 [3] 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]
 [4] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222]
 [5] 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
Functional Description
 Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. 
Sequence Annotation
 MOD_RES 34 34 N6-succinyllysine.
 MOD_RES 51 51 N6-succinyllysine.
 MOD_RES 117 117 N6-acetyllysine; alternate.
 MOD_RES 117 117 N6-succinyllysine; alternate.
 MOD_RES 277 277 N6-succinyllysine.
 MOD_RES 321 321 N6-succinyllysine.
 MOD_RES 390 390 N6-succinyllysine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 548 AA 
Protein Sequence
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI 60
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI 120
DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG 180
TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV 240
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 300
ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY 360
DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI 420
RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA 480
ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG 540
MGGMGGMM 548 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:EcoCyc.
 GO:0016887; F:ATPase activity; IDA:EcoCyc.
 GO:0051082; F:unfolded protein binding; IMP:EcoCyc.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IMP:EcoCyc.
 GO:0042026; P:protein refolding; IEA:HAMAP.
 GO:0009408; P:response to heat; IEP:EcoliWiki.
 GO:0019068; P:virion assembly; IMP:EcoliWiki. 
Interpro
 IPR018370; Chaperonin_Cpn60_CS.
 IPR001844; Chaprnin_Cpn60.
 IPR002423; Cpn60/TCP-1.
 IPR027409; GroEL-like_apical_dom.
 IPR027413; GROEL-like_equatorial. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
 PS00296; CHAPERONINS_CPN60 
PRINTS
 PR00298; CHAPERONIN60.