ID   DNAK_CAMHC              Reviewed;         634 AA.
AC   A7I2D4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=CHAB381_1119;
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000776; ABS51676.1; -; Genomic_DNA.
DR   RefSeq; WP_012108974.1; NC_009714.1.
DR   AlphaFoldDB; A7I2D4; -.
DR   SMR; A7I2D4; -.
DR   STRING; 360107.CHAB381_1119; -.
DR   PRIDE; A7I2D4; -.
DR   EnsemblBacteria; ABS51676; ABS51676; CHAB381_1119.
DR   KEGG; cha:CHAB381_1119; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002407; 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..634
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059531"
FT   REGION          515..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   634 AA;  67530 MW;  FBC4A326DA05D279 CRC64;
     MSKVIGIDLG TTNSCVSVYE RGESKIIPNK EGKNTTPSVV AFTDKGEILV GDSAKRQAVT
     NPEKTIYSIK RIMGLMMNEK NAQEAKKRLP YKIVDRNGAC AVEIAGKVYT PQEISAKVLM
     KLKEDAESYL GEKVVDAVIT VPAYFNDSQR KATKEAGTIA GLNVLRIINE PTAAALAYGL
     DKKESERIVV YDLGGGTFDV TVLETGDSVV EVLATGGNAF LGGDDFDNKL IDYLLSEFKN
     ESGIDIKGDV MAMQRLKEAA ENAKKELSSA METTVNLPFI TADQTGPKHL MKTISRAKFE
     GMIDNLVGET ISTLNSVVSD AGLKMSDIKE VVMVGGSTRV PLVCEEVKKA FGKDLNKSVN
     PDEVVAVGAA VQGAVIKGDV KDVLLLDVTP LSLGIETLGG IMTKLIDKGT TIPTKKSQVF
     STAEDNQSAV TINVLQGERE FARDNKSLGN FNLDGIMPAP RGVPQIEVEF DIDANGILTV
     SAKDKATGKA TDIKITGSSG LSDEEIDKMV KDAELHKEDD KKRKESVDAR NGADAIAHQT
     EKTLNEMGEK IPADLRAKIE AALNDLKAVL KDENATKEQI DAKVSALSKT AEEMYKAASA
     GKNAGGTAGG NGNAGSNGNS GAKKDDDVID AEVE