DNAK_SALTO
ID DNAK_SALTO Reviewed; 613 AA.
AC A4X148;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Strop_0113;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP52598.1; -; Genomic_DNA.
DR RefSeq; WP_011904035.1; NC_009380.1.
DR AlphaFoldDB; A4X148; -.
DR SMR; A4X148; -.
DR STRING; 369723.Strop_0113; -.
DR PRIDE; A4X148; -.
DR EnsemblBacteria; ABP52598; ABP52598; Strop_0113.
DR KEGG; stp:Strop_0113; -.
DR PATRIC; fig|369723.5.peg.112; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_11; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000235; Chromosome.
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; 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..613
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079243"
FT REGION 487..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..586
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 613 AA; 65916 MW; 21F82FAA7F23E831 CRC64;
MARAVGIDLG TTNSCVSVLE GGEPTVIANA EGSRTTPSIV AFARNGEVLV GEVAKRQAVT
NPDRTIRSVK REIGTDWFVD IDDKKYTPQE ISARTLMKLK RDAEAYLGEQ ITDAVITVPA
YFNDGQRQAT KEAGEIAGFN VLRIVNEPTA AALAYGLDKG SKEQTVLVFD LGGGTFDVSL
LELAEGVIEV KSTSGDNLLG GDDWDQRIID HLVKTFNGEH GIDLAQDKMA MQRLKEAAEK
AKIELSAAAT SNINLPYITA GAAGPLHLDV TITRAEFQRM TQDLLDRCKG PFEQAVKDAG
IKVGDVEHVI LVGGSTRMPA VTELVKQLTG RDPNKGVNPD EVVAVGAALQ AGVLKGEVKD
VLLLDVTPLS LGIETKGGIF TKLIERNTTI PTKRSEVFTT ADDNQPSVLI QVFQGEREIA
AYNKKLGTFE LTGLPPAPRG MPQIEVTFDI DANGIVNVHA KDTGTGKEQK MTVTAGSSLP
KEDIERMRRD AEEHAEEDKQ RREEAETRNV AEALQWQTEK FLAESGDKLP TESRDQINEA
LGELRSALGG QDIEKIKSAH AQLAQVSQQA GSQLYTQQQG EQAGATGDQA GAQAGGPDDV
VDAEIVDEDK GKK