CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002951
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chaperone protein DnaK 
Protein Synonyms/Alias
 HSP70; Heat shock 70 kDa protein; Heat shock protein 70 
Gene Name
 dnaK 
Gene Synonyms/Alias
 groP; grpF; seg; b0014; JW0013 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
55TLVGQPAKRQAVTNPacetylation[1]
70QNTLFAIKRLIGRRFacetylation[1]
106GDAWVEVKGQKMAPPacetylation[1, 2]
109WVEVKGQKMAPPQISacetylation[2, 3]
121QISAEVLKKMKKTAEacetylation[1]
166RIAGLEVKRIINEPTacetylation[1]
183ALAYGLDKGTGNRTIacetylation[1, 2]
245NYLVEEFKKDQGIDLacetylation[1, 2, 3]
246YLVEEFKKDQGIDLRacetylation[1]
299GPKHMNIKVTRAKLEacetylation[1, 2]
304NIKVTRAKLESLVEDacetylation[1, 2, 3]
321NRSIEPLKVALQDAGacetylation[2]
351TRMPMVQKKVAEFFGacetylation[1]
359KVAEFFGKEPRKDVNacetylation[1]
363FFGKEPRKDVNPDEAacetylation[1]
421KNTTIPTKHSQVFSTacetylation[1, 2, 3]
452RKRAADNKSLGQFNLacetylation[1]
498KNSGKEQKITIKASSacetylation[1]
502KEQKITIKASSGLNEacetylation[1, 2]
514LNEDEIQKMVRDAEAacetylation[1]
528ANAEADRKFEELVQTacetylation[1, 2]
548HLLHSTRKQVEEAGDacetylation[1, 2]
556QVEEAGDKLPADDKTacetylation[1, 3]
562DKLPADDKTAIESALacetylation[1]
577TALETALKGEDKAAIacetylation[1, 2, 4]
581TALKGEDKAAIEAKMacetylation[1]
587DKAAIEAKMQELAQVacetylation[1]
597ELAQVSQKLMEIAQQacetylation[1, 2]
622DASANNAKDDDVVDAacetylation[1]
635DAEFEEVKDKK****acetylation[1]
635DAEFEEVKDKK****pupylation[5]
637EFEEVKDKK******acetylation[1]
637EFEEVKDKK******pupylation[5]
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] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock. 
Sequence Annotation
 MOD_RES 70 70 N6-succinyllysine.
 MOD_RES 109 109 N6-acetyllysine.
 MOD_RES 199 199 Phosphothreonine; by autocatalysis.
 MOD_RES 245 245 N6-acetyllysine; alternate.
 MOD_RES 245 245 N6-succinyllysine; alternate.
 MOD_RES 246 246 N6-succinyllysine.
 MOD_RES 304 304 N6-acetyllysine; alternate.
 MOD_RES 304 304 N6-succinyllysine; alternate.
 MOD_RES 359 359 N6-succinyllysine.
 MOD_RES 421 421 N6-acetyllysine.
 MOD_RES 502 502 N6-succinyllysine.
 MOD_RES 528 528 N6-succinyllysine.
 MOD_RES 556 556 N6-acetyllysine.
 MOD_RES 587 587 N6-succinyllysine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Cell inner membrane; Cell membrane; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; DNA replication; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 638 AA 
Protein Sequence
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT 60
NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL 120
KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG 180
LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL 240
VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV 300
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE 360
PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT 420
KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA 480
DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD 540
HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME 600
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK 638 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0043531; F:ADP binding; IDA:EcoCyc.
 GO:0005524; F:ATP binding; IDA:EcoCyc.
 GO:0051082; F:unfolded protein binding; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0034620; P:cellular response to unfolded protein; IDA:EcoCyc.
 GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:EcoCyc.
 GO:0051085; P:chaperone mediated protein folding requiring cofactor; IGI:EcoCyc.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0006461; P:protein complex assembly; IDA:EcoCyc.
 GO:0043241; P:protein complex disassembly; IDA:EcoCyc.
 GO:0043335; P:protein unfolding; IDA:EcoCyc.
 GO:0009408; P:response to heat; IDA:EcoCyc. 
Interpro
 IPR012725; Chaperone_DnaK.
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 
Pfam
 PF00012; HSP70 
SMART
  
PROSITE
 PS00297; HSP70_1
 PS00329; HSP70_2
 PS01036; HSP70_3 
PRINTS
 PR00301; HEATSHOCK70.