ID   DNAK1_ALIF1             Reviewed;         632 AA.
AC   Q5E4T4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Chaperone protein DnaK 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 1 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK1 {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=VF_1467;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85962.1; -; Genomic_DNA.
DR   RefSeq; WP_011262053.1; NC_006840.2.
DR   RefSeq; YP_204850.1; NC_006840.2.
DR   AlphaFoldDB; Q5E4T4; -.
DR   SMR; Q5E4T4; -.
DR   STRING; 312309.VF_1467; -.
DR   PRIDE; Q5E4T4; -.
DR   EnsemblBacteria; AAW85962; AAW85962; VF_1467.
DR   KEGG; vfi:VF_1467; -.
DR   PATRIC; fig|312309.11.peg.1484; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; DKMVLQR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000537; 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   Reference proteome; Stress response.
FT   CHAIN           1..632
FT                   /note="Chaperone protein DnaK 1"
FT                   /id="PRO_0000226026"
FT   REGION          601..632
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   632 AA;  68364 MW;  62549A8462D61345 CRC64;
     MGKIIGIDLG TTNSCVAVLD GDTPRILENA EGERTTASVI AYTDGETLVG QPAKRQAITN
     PQNTLFAIKR LIGRRFEDEE VQRDIEIMPY KIIKADNGDA WVEAKGQKMA APQVSAEILK
     KMKKTAEDFL GEEVTGAVVT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAAALAYGL
     DKKGGDRTIA VYDLGGGTFD ISIIEIDNVD GEQTFEVLAT NGDTHLGGED FDNRLINFLV
     DEFKKEQGFD LKNDPLAMQR VKEAAEKAKI ELSSAQQTDV NLPYVTADAT GPKHMNIKVT
     RAKLESLVED LVVRTLEPLK VALADADLTI DGITDVILVG GQTRMPMVQA KVAEFFGKEA
     RRDVNPDEAV AMGAAVQGGV LAGDVKDVLL LDVTPLSFGI ETMGGVMTKL IEKNTTIPTK
     ADQTFSTAED NQSAVTIHVL QGERKQASYN KSLGQFNLEG IQAAPRGMPQ IEVTFDLDAD
     GILNVSAKDK STGKEQKITI QASGGLTDEE IEAMVQEAEA NKDADKKFEE LVTARNQADQ
     MIHGTKKQIE EAGDDLPTDE KEKIEAAITA LEGVKSGDDK EAIDAKTQEL MQAAQKLMEI
     AQQKAQAQQG AQAGEQPKQE DDVVDAEFEE VK