(data stored in ACNUC7421 zone)

SWISSPROT: B7UI59_ECO27

ID   B7UI59_ECO27            Unreviewed;       638 AA.
AC   B7UI59;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332,
GN   ECO:0000313|EMBL:CAS07562.1};
GN   OrderedLocusNames=E2348C_0014 {ECO:0000313|EMBL:CAS07562.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07562.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07562.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000256|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock.
CC       {ECO:0000256|HAMAP-Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00332, ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; FM180568; CAS07562.1; -; Genomic_DNA.
DR   RefSeq; WP_000516135.1; NC_011601.1.
DR   SMR; B7UI59; -.
DR   EnsemblBacteria; CAS07562; CAS07562; E2348C_0014.
DR   KEGG; ecg:E2348C_0014; -.
DR   HOGENOM; HOG000228136; -.
DR   KO; K04043; -.
DR   OMA; ISIKRHM; -.
DR   BioCyc; ECOL574521:E2348C_RS00075-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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_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   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   2: Evidence at transcript level;
DR   PRODOM; B7UI59.
DR   SWISS-2DPAGE; B7UI59.
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_00332};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00332,
KW   ECO:0000256|RuleBase:RU003322};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00332};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00332,
KW   ECO:0000256|RuleBase:RU003322};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00332};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00332}.
FT   COILED      259    279       {ECO:0000256|SAM:Coils}.
FT   COILED      584    604       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     109    109       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00332}.
FT   MOD_RES     199    199       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00332}.
FT   MOD_RES     245    245       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00332}.
FT   MOD_RES     304    304       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00332}.
FT   MOD_RES     421    421       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00332}.
FT   MOD_RES     556    556       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00332}.
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
//

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