ID   DNAK_CAMC1              Reviewed;         623 AA.
AC   A7ZEB5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Ccon26_12700; ORFNames=CCC13826_2046;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-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; CP000792; EAT98798.1; -; Genomic_DNA.
DR   RefSeq; WP_012140035.1; NC_009802.2.
DR   AlphaFoldDB; A7ZEB5; -.
DR   SMR; A7ZEB5; -.
DR   STRING; 360104.CCC13826_2046; -.
DR   PRIDE; A7ZEB5; -.
DR   EnsemblBacteria; EAT98798; EAT98798; CCC13826_2046.
DR   KEGG; cco:CCC13826_2046; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001121; 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   Stress response.
FT   CHAIN           1..623
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000072033"
FT   REGION          600..623
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   623 AA;  66939 MW;  EDECFC51650AA7A4 CRC64;
     MSKVIGIDLG TTNSCVSVFE RGESKVIPNK EGKNTTPSVV AFTDKGEILV GDVAKRQAVT
     NPEKTIYSIK RIMGLMSNEK NAEEAKARLP YHVVDRNGAC AVEIAGKVYT PQEISAKILI
     KLKEDAEAYL GESVTDAVIT VPAYFNDSQR KATKEAGTIA GLNVLRIINE PTAAALAYGL
     DKKEAEKILV YDLGGGTFDV TVLETGDNIV EVLATGGNAF LGGDDFDNKI IDWLVSEFKN
     ETGIDLKGDI MALQRLKEAA ENAKKELSSA QETEINLPFI TADATGPKHL VKKLTRAKFE
     GMIDSLVGET ITKINEVIKD AGLSKSDIKE VVMVGGSTRV PLVQEEVKKA FGKELNKSVN
     PDEVVAIGAA IQGAVIKGDV KDVLLLDVTP LSLGIETLGG VMTKIIEKGT TIPTKKSQVF
     STAEDNQNAV TIMVLQGERE FARDNKSLGN FNLEGIPAAP RGVPQIEVEF DIDANGILTV
     SAKDKATGKA QNITISGSSG LSEDEINSMV KDAELHKEED KKRKDAVEAR NQADALVHQT
     EKSMSELGEK VPAEDRSNIE AALNDLKEVL KDENSSKEQI DAKVEALSKA SHKLAEAMYK
     KDENAGANGG NKKDDDVIDA EVE