(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 77.
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}.
DR   EMBL; CP000667; ABP52598.1; -; Genomic_DNA.
DR   RefSeq; WP_011904035.1; NC_009380.1.
DR   SMR; A4X148; -.
DR   STRING; 369723.Strop_0113; -.
DR   PRIDE; A4X148; -.
DR   EnsemblBacteria; ABP52598; ABP52598; Strop_0113.
DR   GeneID; 5056546; -.
DR   KEGG; stp:Strop_0113; -.
DR   PATRIC; fig|369723.5.peg.112; -.
DR   eggNOG; ENOG4105CFG; Bacteria.
DR   eggNOG; COG0443; LUCA.
DR   HOGENOM; HOG000228137; -.
DR   KO; K04043; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000235; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
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   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;
DR   PRODOM; A4X148.
DR   SWISS-2DPAGE; A4X148.
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   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
//

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