ID   DNAK_VIBA3              Reviewed;         637 AA.
AC   B7VJW9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=VS_0651;
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32;
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FM954972; CAV17645.1; -; Genomic_DNA.
DR   RefSeq; WP_009848331.1; NC_011753.2.
DR   AlphaFoldDB; B7VJW9; -.
DR   SMR; B7VJW9; -.
DR   STRING; 575788.VS_0651; -.
DR   PRIDE; B7VJW9; -.
DR   EnsemblBacteria; CAV17645; CAV17645; VS_0651.
DR   KEGG; vsp:VS_0651; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000009100; Chromosome 1.
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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000133171"
FT   REGION          601..637
FT                   /note="Disordered"
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   637 AA;  68903 MW;  7465EB71A1B124F5 CRC64;
     MGRIIGIDLG TTNSCVAVLD GDKPRVLENA EGERTTASVI AYTEGETLVG QPAKRQAVTN
     PQNTLYAIKR LIGRRFEDEE VQRDIEIMPF NIVKADNGDA WVEAQGQKMA APQVSAEVLK
     KMKKTAEDFL GEEVTGAVVT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAAALAYGL
     DKQGGDRTIA VYDLGGGTFD ISIIEIDEVE GEKTFEVLST NGDTHLGGED FDNRMINYLV
     DEFKKEQGID LKADPLAMQR VKEAAEKAKI ELSSTTQTDV NLPYVTADAT GPKHMNIKVT
     RAKLESLVED LVQRSLEPLK VALADADLSV GEITDVILVG GQTRMPMVQA KVTEFFGKEP
     RKDVNPDEAV AMGAAVQGGV LAGEVKDVLL LDVTPLSFGI ETMGGVMTKL IEKNTTIPTK
     ADQVFSTAED NQSAVTIHVL QGERKQATYN KSLGQFNLEG IQPAPRGMPQ VEVTFDLDAD
     GILNVSAKDK ATGKEQKITI QASGGLSEEE IEAMVQEAEA NKEADKKFEE LVTARNQADQ
     MIHGTKKQVE EAGEALPADE KAKIEAAIEA LESVKSGDDK EAIDAKVQEL MQAAQKLMEI
     AQQKAQAEQA GADAGEQPKQ DDDVVDAEFE EVKEDKK