ID   DNAK_SALRD              Reviewed;         667 AA.
AC   Q2S307;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=SRU_1300;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(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; CP000159; ABC44636.1; -; Genomic_DNA.
DR   RefSeq; WP_011404052.1; NC_007677.1.
DR   RefSeq; YP_445424.1; NC_007677.1.
DR   AlphaFoldDB; Q2S307; -.
DR   SMR; Q2S307; -.
DR   STRING; 309807.SRU_1300; -.
DR   EnsemblBacteria; ABC44636; ABC44636; SRU_1300.
DR   KEGG; sru:SRU_1300; -.
DR   PATRIC; fig|309807.25.peg.1351; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_10; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000008674; 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; 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..667
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059656"
FT   REGION          495..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..667
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   667 AA;  71332 MW;  8948D1B5C40E1D0C CRC64;
     MGKVIGIDLG TTNSVVAVME GDDPEVIENA EGSRTTPSVV AYKDDGERLV GAPAKRQAIT
     NPENTVSSIK RFMGRFYDEV EDEIEEVPYE VVRGENDTAR VQIGDRKYTP QEISAVVLQK
     LKQTAEDYLG QEVTDAVITV PAYFNDAQRK ATQEAGEIAG LNVQRIINEP TAASLAYGLD
     DESDQVVAVY DLGGGTFDVS ILELGDGVFE VNATYGDTHL GGDNFDKRLI DHIADEFEQD
     TGIDLRDDPM ALQRLKEAAE EAKIELSSAK TTTINLPFIT ATDEGPQHLN MDLNRATFEN
     LIEDLVEKTV PQMEKALDDA GHSKSDVDEV ILVGGSTRVP LVQETVEDFF GKQANKSVNP
     DEVVSLGAAV QGGVLSGDVD DVLLLDVTPL NLGIETLGGV MTTLIEANTT IPTKESEVFS
     TAADNQTSVE VHVLQGDREM AKDNRTLGRF HLDGIPPAPR GTPQIEVTFD INADGILNVS
     AEDKDTGKEQ SIRVEANSGL SDEEIEKMKE EAEQHAEEDE RRKERADTIN EANSMAYSVE
     QGLEEYGDKI PEDKRSTLQE ALDALNEELE TASADEDITA LEDALEELNA AWSAAGEEIR
     EAQQQQAQQG AAAGAGAGAA GAGAAAGAEG PAGGPTGGPA SGNGAADSDE EDVQDADYEV
     VDEGDDE