ID   DNAK2_ALIF1             Reviewed;         634 AA.
AC   Q5E3A7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Chaperone protein DnaK 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 2 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK2 {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=VF_1994;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000020; AAW86489.1; -; Genomic_DNA.
DR   RefSeq; WP_011262456.1; NC_006840.2.
DR   RefSeq; YP_205377.1; NC_006840.2.
DR   AlphaFoldDB; Q5E3A7; -.
DR   SMR; Q5E3A7; -.
DR   STRING; 312309.VF_1994; -.
DR   EnsemblBacteria; AAW86489; AAW86489; VF_1994.
DR   KEGG; vfi:VF_1994; -.
DR   PATRIC; fig|312309.11.peg.2021; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
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..634
FT                   /note="Chaperone protein DnaK 2"
FT                   /id="PRO_0000226027"
FT   REGION          602..634
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   634 AA;  68540 MW;  86DE9A2B18300212 CRC64;
     MGKIIGIDLG TTNSCVAVLD GDTPRVLENA EGERTTASVI AYTDGETLVG QPAKRQAVTN
     PQNTLFAIKR LIGRRFEDEE VQRDIEIMPF KIVKADNGDA WVEAKGQKMA APQVSAEVLK
     KMKKTAEDFL GEEVTGAVVT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAAALAYGL
     DKKGGDRTIA VYDLGGGTFD ISIIEIDNVD GEQTFEVLAT NGDTHLGGED FDNRLINYLV
     SEFEKEQGIN LKNDPLAMQR VKEAAEKAKI ELSSAQQTDV NLPYVTADAT GPKHMNVKVT
     RAKLESLVED LVLRSLEPLK VALADADLSV DEITDVILVG GQTRMPMVQA KVAEFFGKEA
     RRDVNPDEAV AMGAAVQGGV LAGDVKDVLL LDVTPLSFGI ETMGGVMTKL IEKNTTIPTK
     ADQTFSTAED NQSAVTIHVL QGERKQATYN KSLGQFNLEG IQPAPRGMPQ IEVTFDLDAD
     GILNVSAKDK ATGKEQKITI QASGGLTDEE IEAMVQEAEA NKDADKKFEE LVTARNQADQ
     MIHGTQKQIE EAGDALPADE KEKIEAAIKA LEEVKSGNDK EAIDAKTQEL MQAAQKLMEI
     AQQKAQAQQG ADAGEQPKQD DDVVDAEFEE VKDK