DNAK_VIBCM
ID DNAK_VIBCM Reviewed; 635 AA.
AC C3LTA5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=VCM66_0812;
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP001233; ACP05131.1; -; Genomic_DNA.
DR RefSeq; WP_000516147.1; NC_012578.1.
DR AlphaFoldDB; C3LTA5; -.
DR SMR; C3LTA5; -.
DR EnsemblBacteria; ACP05131; ACP05131; VCM66_0812.
DR GeneID; 57739554; -.
DR KEGG; vcm:VCM66_0812; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001217; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..635
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133170"
FT REGION 601..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 635 AA; 68761 MW; 2A05D6F5411EC953 CRC64;
MGKIIGIDLG TTNSCVAVLD GDKPRVIENA EGERTTPSVI AYTDGETLVG QPAKRQAVTN
PQNTLFAIKR LIGRRFEDEE VQRDIKIMPY KIVKADNGDA WVEAKGQKMA APQVSAEVLK
KMKKTAEDFL GEPVTAAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAAALAYGL
DKQGGDRTIA VYDLGGGTFD ISIIEIDEVE GEKTFEVLST NGDTHLGGED FDNRMINYLV
DEFKKDQGID LRNDPLAMQR LKEAAEKAKI ELSSAQQTDV NLPYITADAT GPKHMNIKVT
RAKLEALVED LVQRSLEPLK VALADADLSV NDITDVILVG GQTRMPMVQK KVAEFFGKEP
RKDVNPDEAV AVGAAVQGGV LAGEVKDVLL LDVTPLSLGI ETMGGVMTKL IEKNTTIPTK
ANQVFSTAED NQSAVTIHVL QGERKQAMYN KSLGQFNLEG INPAPRGMPQ IEVIFDLDAD
GILHVSAKDK QTGKEQKITI QASGGLSDAE IEKMVQEAEA NKEADKKFEE LATARNQADQ
MIHATRKQIT EAGEALPADE KAKIETAINE LETAKKGEDK AEIDAKVQAL MAAAQKLMEI
AQQQAQAQGA NAGQSSAKED DVVDAEFEEV NDDKK