ID   DNAK_STAS1              Reviewed;         614 AA.
AC   Q49Y22;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=SSP1177;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18322.1; -; Genomic_DNA.
DR   RefSeq; WP_002483153.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49Y22; -.
DR   SMR; Q49Y22; -.
DR   STRING; 342451.SSP1177; -.
DR   PRIDE; Q49Y22; -.
DR   EnsemblBacteria; BAE18322; BAE18322; SSP1177.
DR   GeneID; 66867406; -.
DR   KEGG; ssp:SSP1177; -.
DR   PATRIC; fig|342451.11.peg.1175; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006371; 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; 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..614
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000226013"
FT   REGION          490..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   614 AA;  66585 MW;  5F366C9DA41A3E9E CRC64;
     MSKVIGIDLG TTNSCIAILE GDEPKVIQNP EGARTTPSVV AFKNDETQVG EVAKRQAITN
     PNTIQSIKRH MGTDYKVDVD GKSYTPQEIS AMVLQNLKST AEDYLGESVD KAVITVPAYF
     NDSERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTEQ DQKVLVFDLG GGTFDVSILE
     LGDGVFEVLS TAGDNKLGGD DFDQVIIDHL VAEFKKENSV DLSKDKMALQ RLKDAAEKAK
     KDLSGVSQTQ ISLPFISAGE NGPLHLELTL TRSKFEELAD SLIRRTMEPT RQAMKDAGLS
     SSDIDEVILV GGSTRIPAVQ EAVKKEVGKD PHKGVNPDEV VAMGAAIQGG VITGDVKDVV
     LLDVTPLSLG IEIMGGRMNT LIERNTTIPT SKSQVYSTAA DNQPAVDIHV LQGERPMAAD
     NKTLGRFQLT DIPAAPRGVP QIEVTFDIDK NGIVNVTAKD LGTNKEQNIT IQSSSALSDD
     EIDRMVKDAE ENAEADKKRR EESDLRNEAD SLVFQVEKTI TDLGENISEE DKQNAEDKKE
     ALKSALEGED IDDIKAKKED LEKVVQDLST KVYEQAAQAQ QQAQGEDANA SQDSNVEDAD
     FKEVKDDDNQ DNQK