ID DNAK_CAMFF Reviewed; 626 AA.
AC A0RPW7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=CFF8240_1089;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) 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; CP000487; ABK81904.1; -; Genomic_DNA.
DR RefSeq; WP_011732077.1; NC_008599.1.
DR AlphaFoldDB; A0RPW7; -.
DR SMR; A0RPW7; -.
DR GeneID; 61064916; -.
DR KEGG; cff:CFF8240_1089; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_7; -.
DR Proteomes; UP000000760; 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 CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375:SF541; CHAPERONE PROTEIN DNAK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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..626
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059530"
FT REGION 512..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..626
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 626 AA; 67117 MW; 4FD8AF1BF0BDB320 CRC64;
MSKVIGIDLG TTNSCVSIYE RGESKVIPNK EGKNTTPSVV AFTDKGEILV GDTAKRQAVT
NPEKTIFSIK RIMGLMMNEK NAKEAKNRLP YHIVDRNGAC AVEIAGKTYT PQEISAKVLM
KLKEDAEAFL GESVVDAVIT VPAYFNDSQR KATKEAGTIA GLNVLRIINE PTAAALAYGL
DKKEAEKIVV YDLGGGTFDV TVLETGDSVV EVLATGGNAF LGGDDFDNRL IDFLVSEFKS
ETGIDLKNDV MALQRLKEAA ENAKKELSSA METTINLPFI TADATGPKHL TKTLSRAKFE
GMIDDLVGET ITKINEVVKD AGISKGDIKE VVMVGGSTRV PLVQEEVKKA FSKELNKSVN
PDEVVAIGAA IQGAVIKGDV KDVLLLDVTP LSLGIETLGG VMSKLIEKGT TIPTKKSQTF
STAEDNQSAV TINVLQGERE FAKDNKSLGN FNLEGIMPAP RGVPQIEVTF DIDANGILTV
SAKDKASGKA QNITISGSSG LSEEEINKMV NDAEAHKEDD KKRKEAVEAR NAADSLAHQT
EKSLSEMGEK IPAEDRAKIE AALNDLKEVL KDESASKEQI DVKVKALSEV SHKLAEAMYK
DQNAGAADGG AEKKKKDDDV IDAEVE
//
