DNAK_CAMJR
ID DNAK_CAMJR Reviewed; 623 AA.
AC Q5HV33;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=CJE0850;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
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; CP000025; AAW35187.1; -; Genomic_DNA.
DR RefSeq; WP_002856760.1; NC_003912.7.
DR AlphaFoldDB; Q5HV33; -.
DR SMR; Q5HV33; -.
DR PRIDE; Q5HV33; -.
DR KEGG; cjr:CJE0850; -.
DR HOGENOM; CLU_005965_2_4_7; -.
DR OMA; ISIKRHM; -.
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 GO; GO:0009408; P:response to heat; IDA:TIGR.
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_0000225947"
FT REGION 595..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; 67416 MW; 034B64FE0D977505 CRC64;
MSKVIGIDLG TTNSCVAVYE RGESKVIPNK EGKNTTPSVV AFTDKGEVLV GDSAKRQAVT
NPEKTIYSIK RIMGLMINED AAKEAKNRLP YHITERNGAC AIEIAGKIYT PQEISAKVLM
KLKEDAEAFL GESVVDAVIT VPAYFNDAQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
DKKDSEKIVV YDLGGGTFDV TVLETGDNVV EVLATGGNAF LGGDDFDNKL IDFLANEFKD
ETGIDLKNDV MALQRLKEAA ENAKKELSSA NETEINLPFI TADASGPKHL VKKLTRAKFE
GMIDSLVAET ITKINEVVSD AGLKKDEIKE IVMVGGSTRV PLVQEEVKKA FNKDLNKSVN
PDEVVAIGAA IQGAVIKGDV KDVLLLDVTP LSLGIETLGG VMTKIIEKGT TIPTKKEQVF
STAEDNQSAV TINVLQGERE FSRDNKSLGN FNLEGIPPAP RGMPQIEVTF DIDANGILTV
SAKDKATGKA QEIKITGSSG LSEEEINNMV KDAELHKEED KKRKEAVDAR NAADSLAHQV
EKSLSELGEK VAAADKENIQ KALDDLRETL KNQNASKEEI ESKMKALSEV SHKLAENMYK
KDEPNTANDK KKKDDDVIDA EVE