ID DNAK_CAMJE Reviewed; 623 AA.
AC O69298; Q0PAD1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 01-MAY-2013, entry version 80.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=Cj0759;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10024560;
RA Thies F., Karch H., Hartung H.P., Giegerich G.;
RT "Cloning and expression of the dnaK gene of Campylobacter jejuni and
RT antigenicity of heat shock protein 70.";
RL Infect. Immun. 67:1194-1200(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
RA Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA Whitehead S., Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: Acts as a chaperone (By similarity).
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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DR EMBL; Y17165; CAA76670.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL34887.1; -; Genomic_DNA.
DR PIR; G81346; G81346.
DR RefSeq; YP_002344166.1; NC_002163.1.
DR ProteinModelPortal; O69298; -.
DR SMR; O69298; 1-596.
DR STRING; 192222.Cj0759; -.
DR EnsemblBacteria; CAL34887; CAL34887; Cj0759.
DR GeneID; 905069; -.
DR KEGG; cje:Cj0759; -.
DR PATRIC; 20058466; VBICamJej33762_0747.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228135; -.
DR KO; K04043; -.
DR OMA; VAIMDGA; -.
DR ProtClustDB; PRK00290; -.
DR BioCyc; CJEJ192222:GJTS-733-MONOMER; -.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR HAMAP; MF_00332; DnaK; 1; -.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
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; Complete proteome; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1 623 Chaperone protein DnaK.
FT /FTId=PRO_0000078438.
FT MOD_RES 197 197 Phosphothreonine; by autocatalysis (By
FT similarity).
SQ SEQUENCE 623 AA; 67418 MW; CB6CF827C00BACC8 CRC64;
MSKVIGIDLG TTNSCVAVYE RGESKVIPNK EGKNTTPSVV AFTDKGEVLV GDSAKRQAVT
NPEKTIYSIK RIMGLMINED AAKEAKNRLP YHITERNGAC AIEIAGKIYT PQEISAKVLM
KLKEDAEAFL GESVTDAVIT 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
//
