ID   DNAK_CAMC5              Reviewed;         625 AA.
AC   A7GXU4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Ccur92_07320; ORFNames=CCV52592_0148;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
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; CP000767; EAU00227.1; -; Genomic_DNA.
DR   RefSeq; WP_009650189.1; NC_009715.2.
DR   AlphaFoldDB; A7GXU4; -.
DR   SMR; A7GXU4; -.
DR   STRING; 360105.CCV52592_0148; -.
DR   PRIDE; A7GXU4; -.
DR   EnsemblBacteria; EAU00227; EAU00227; CCV52592_0148.
DR   GeneID; 61002035; -.
DR   KEGG; ccv:CCV52592_0148; -.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006380; 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..625
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059529"
FT   REGION          598..625
FT                   /note="Disordered"
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   625 AA;  67220 MW;  C15B1A3E074E9673 CRC64;
     MAKVIGIDLG TTNSCVSVYE RGESKVIPNK EGKNTTPSVV AFTDKGEVLV GDVAKRQAVT
     NPEKTIYSIK RIMGLMSNEK NAQEAKARLP YHVVDRNGAC AVEIAGKVYT PQEISAKILM
     KLKEDAEAYL GEKVVDAVIT VPAYFNDSQR KATKEAGTIA GLNVLRIINE PTAAALAYGL
     DKKEAEKILV YDLGGGTFDV TVLETGDSVV EVLATGGNAF LGGDDFDNLI IDWLVNEFKN
     ETGIDLKKDV MASQRLKEAA ENAKKELSSA QETEINLPFI TADATGPKHL VKKLTRAKFE
     GMIESLVAET ITKINEVVKE AGLSKSDVKE VVMVGGSTRV PLVQEEVKKA FGKELNKSVN
     PDEVVAIGAA IQGAVIKGDV KDVLLLDVTP LSLGIETLGG VMTKIIEKGT TIPVKKNQTF
     STAEDNQSAV TIHVLQGERE FARDNKSLGQ FNLEGIPSAP RGVPQIEVEF DIDANGILTV
     SAKDKATGKA QNITISGSSG LSEDEINNMV KDAELHKEDD KKRKEAVEAR NSADALVHQT
     EKSMNELGEK VPAEDRSNIE AALNDLKETL KDENASKEQI DAKVQALSAA SHKLAEAMYK
     KDDNASGEQS GGKKKDDDVI DAEVE