DNAK_VIBCH
ID DNAK_VIBCH Reviewed; 635 AA.
AC O34241; Q9KTP6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=VC_0855;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RX PubMed=10024539; DOI=10.1128/iai.67.3.1025-1033.1999;
RA Chakrabarti S., Sengupta N., Chowdhury R.;
RT "Role of DnaK in in vitro and in vivo expression of virulence factors of
RT Vibrio cholerae.";
RL Infect. Immun. 67:1025-1033(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; Y14237; CAA74627.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF94017.1; -; Genomic_DNA.
DR PIR; B82273; B82273.
DR RefSeq; NP_230502.1; NC_002505.1.
DR RefSeq; WP_000516147.1; NZ_LT906614.1.
DR AlphaFoldDB; O34241; -.
DR SMR; O34241; -.
DR STRING; 243277.VC_0855; -.
DR PRIDE; O34241; -.
DR DNASU; 2614522; -.
DR EnsemblBacteria; AAF94017; AAF94017; VC_0855.
DR GeneID; 57739554; -.
DR KEGG; vch:VC_0855; -.
DR PATRIC; fig|243277.26.peg.816; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR BioCyc; VCHO:VC0855-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 Reference proteome; Stress response.
FT CHAIN 1..635
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078581"
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:0000250"
FT CONFLICT 46..47
FT /note="ET -> VS (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="Q -> P (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="G -> C (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="Q -> P (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="Y -> H (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="D -> E (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="L -> Q (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..397
FT /note="PLS -> LLF (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="L -> F (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="A -> R (in Ref. 1; CAA74627)"
FT /evidence="ECO:0000305"
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
