(data stored in ACNUC7421 zone)

SWISSPROT: DNAK_ECO57

ID   DNAK_ECO57              Reviewed;         638 AA.
AC   P0A6Z0; P04475;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-JUL-2017, entry version 87.
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=Z0014, ECs0014;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000305}.
DR   EMBL; AE005174; AAG54314.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33437.1; -; Genomic_DNA.
DR   PIR; F85481; F85481.
DR   PIR; F90630; F90630.
DR   RefSeq; NP_308041.1; NC_002695.1.
DR   RefSeq; WP_000516135.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; P0A6Z0; -.
DR   SMR; P0A6Z0; -.
DR   MINT; MINT-1216219; -.
DR   STRING; 155864.Z0014; -.
DR   PRIDE; P0A6Z0; -.
DR   EnsemblBacteria; AAG54314; AAG54314; Z0014.
DR   EnsemblBacteria; BAB33437; BAB33437; BAB33437.
DR   GeneID; 913406; -.
DR   KEGG; ece:Z0014; -.
DR   KEGG; ecs:ECs0014; -.
DR   PATRIC; fig|386585.9.peg.110; -.
DR   eggNOG; ENOG4105CFG; Bacteria.
DR   eggNOG; COG0443; LUCA.
DR   HOGENOM; HOG000228136; -.
DR   KO; K04043; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C.
DR   InterPro; IPR029047; HSP70_peptide-bd.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
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;
DR   PRODOM; P0A6Z0.
DR   SWISS-2DPAGE; P0A6Z0.
KW   Acetylation; ATP-binding; Chaperone; Complete proteome;
KW   Nucleotide-binding; Phosphoprotein; Stress response.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    638       Chaperone protein DnaK.
FT                                /FTId=PRO_0000078460.
FT   MOD_RES     109    109       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     199    199       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     245    245       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     304    304       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     421    421       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     556    556       N6-acetyllysine. {ECO:0000250}.
SQ   SEQUENCE   638 AA;  69115 MW;  5A8589B21D7CD9C1 CRC64;
     MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT
     NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL
     KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
     LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL
     VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
     TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE
     PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT
     KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA
     DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD
     HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME
     IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK
//

If you have problems or comments...

PBIL Back to PBIL home page