DNAK_CAMLR
ID DNAK_CAMLR Reviewed; 622 AA.
AC B9KCH0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Cla_0935;
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
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; CP000932; ACM64259.1; -; Genomic_DNA.
DR RefSeq; WP_012661642.1; NC_012039.1.
DR AlphaFoldDB; B9KCH0; -.
DR SMR; B9KCH0; -.
DR STRING; 306263.Cla_0935; -.
DR PRIDE; B9KCH0; -.
DR EnsemblBacteria; ACM64259; ACM64259; CLA_0935.
DR GeneID; 7410515; -.
DR KEGG; cla:CLA_0935; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000007727; 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..622
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133137"
FT REGION 515..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..622
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 622 AA; 67388 MW; 4E6E45606A0298F7 CRC64;
MSKVIGIDLG TTNSCVSVYE RGESKVIPNK EGKNTTPSVV AFTDKGEILV GDSAKRQAVT
NPEKTIYSIK RIMGLMINED AAKEAKNRLP YHITERNGAC AIEIAGKIYT PQEISAKVLM
KLKEDAEAFL GEKVEDAVIT VPAYFNDAQR KATKEAGTIA GLNVLRIINE PTAAALAYGL
DKKESEKIVV YDLGGGTFDV TVLETGDNVV EVLATGGNAF LGGDDFDNKL IDYLASEFKD
ETGIDLKNDV MALQRLKEAA ENAKKELSSA NETNVNLPFI TADASGPKHL TKTITRAKFE
SMIDGLVAET ISKINEVVKD AGLDKSEVKE IVMVGGSTRV PLVQEEVKKA FGKDLNKSVN
PDEVVAIGAA IQGAVIKGDV KDVLLLDVTP LSLGIETLGG VMTKIIEKGT TIPTKKEQTF
STAEDNQSAV TINVLQGERE FSRDNKSLGN FNLEGIPPAP RGMPQIEVTF DIDANGILTV
SAKDKATGKA QEIKITGSSG LSEEEINNMV KDAELHKEED RKRKEAVEAR NSADSLVHQV
EKSLSELGEK VSDEDKANIQ KALDDLKETL KNANASKEEI ESKMKTLSEV SHKLAENMYK
KDEKPSDDKK KKDDDVIDAE VE