ID   DNAK_SALAI              Reviewed;         611 AA.
AC   A8LWM4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Sare_0112;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) 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; CP000850; ABV96047.1; -; Genomic_DNA.
DR   RefSeq; WP_012180360.1; NC_009953.1.
DR   AlphaFoldDB; A8LWM4; -.
DR   SMR; A8LWM4; -.
DR   STRING; 391037.Sare_0112; -.
DR   PRIDE; A8LWM4; -.
DR   EnsemblBacteria; ABV96047; ABV96047; Sare_0112.
DR   GeneID; 5707040; -.
DR   KEGG; saq:Sare_0112; -.
DR   PATRIC; fig|391037.6.peg.118; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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; 2.
DR   Pfam; PF00012; HSP70; 2.
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..611
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000079240"
FT   REGION          467..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   611 AA;  65628 MW;  9D35E930DE9C83C0 CRC64;
     MARAVGIDLG TTNSCVSVLE GGEPTVIANA EGSRTTPSIV AFARNGEVLV GEVAKRQAVT
     NPDRTIRSVK REVGTNWSVD IDDKKYTPQE ISARTLMKLK RDAESYLGEQ ITDAVITVPA
     YFNDGQRQAT KEAGEIAGFN VLRIVNEPTA AALAYGLDKG SKEQTVLVFD LGGGTFDVSL
     LELAEGVIEV KSTSGDNLLG GDDWDQRIID HLVKTFNGEH GIDLSQDKMA MQRLKEAAEK
     AKIELSAAAT SNINLPYITA GAAGPLHLDV TLTRAEFQRM TQDLLDRCKG PFEQAVKDAG
     IKVADVEHVI LVGGSTRMPA VTELVKDLTG RDPNKGVNPD EVVAVGAALQ AGVLKGEVKD
     VLLLDVTPLS LGIETKGGIF TKLIERNTTI PTKRSEVFTT ADDNQPSVLI QVFQGEREIA
     AYNKKLGTFE LTGLPPAPRG MPQIEVTFDI DANGIVNVHA KDLGTGKEQK MTVTAGSSLP
     KEDIERMRRD AEEHAEEDKR RREEAETRNL AEALQWQTEK FLAESGDKLP TESRDQINEA
     LGELRSALGG QDIEKIKSAH AQLAQVSQQA GSQLYTQQGE QAGATGAQAG GAQAGGPDDV
     VDAEIVDEDK K