ID   DNAK_CARRP              Reviewed;         602 AA.
AC   Q05FS8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=CRP_062;
OS   Carsonella ruddii (strain PV).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX   NCBI_TaxID=387662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV;
RX   PubMed=17038615; DOI=10.1126/science.1134196;
RA   Nakabachi A., Yamashita A., Toh H., Ishikawa H., Dunbar H.E., Moran N.A.,
RA   Hattori M.;
RT   "The 160-kilobase genome of the bacterial endosymbiont Carsonella.";
RL   Science 314:267-267(2006).
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; AP009180; BAF35093.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05FS8; -.
DR   SMR; Q05FS8; -.
DR   STRING; 387662.CRP_062; -.
DR   EnsemblBacteria; BAF35093; BAF35093; CRP_062.
DR   KEGG; crp:CRP_062; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000777; 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; 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..602
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059533"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   602 AA;  66120 MW;  49A288000E2DD30C CRC64;
     MSKIIGIDLG TTNSCIAVLS NGKPQVIENS EGGRTTPSVV GYTEDNRIIV GLPAKRQAIT
     NPKNTLYAIK RLIGRKFKDD IVQKDIKMVP YKIISSENGD AWVEVKDKKL APPQISAEIL
     KKMKITAENF LNEKVTKAVI TVPAYFNDSQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKKKNDRII AVYDLGGGTF DISIIEIANV DGETQFEVLS TNGDTFLGGE DFDIRIINNL
     IYEFKIENGI NLSGDSLAMQ RLKEAAEKAK IELSSVEQTD INLPYITADK NGPKHLNIKI
     TRSKLESLVE DLILKSLKPC EIALNDAKIS KNKIDEIILV GGQTRMPLVQ KMVSDFFEKV
     VKKDINPDEA VAIGASVQAG VLSGVVKDVL LLDVTPLTLG IETMGGIMTP LIEKNTTIPT
     KKTQVFSTAE DNQTSVTIHT LQGERKKALQ NKSLGKFDLN NISPAPRGVP QIEVSFDLDA
     NGILNVTAKD KKTGVEQSIV IKSSGGLSEL EIENMIKDAE ANLEIDKKFE ELVKCRNEAD
     STISIVKKKL KDENLKILDE ERVSIEKSIS NLELLIKGDD IDSIKKENEE LLKLSDNIIK
     KK