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Database: UniProt
Entry: O69298
LinkDB: O69298
Original site: O69298 
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   19-FEB-2014, entry version 83.
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; CELSSSQ; -.
DR   OrthoDB; EOG6JMMSV; -.
DR   ProtClustDB; PRK00290; -.
DR   BioCyc; CJEJ192222:GJTS-733-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-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
//
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