(data stored in ACNUC7421 zone)

SWISSPROT: DNAK_ECOL5

ID   DNAK_ECOL5              Reviewed;         638 AA.
AC   Q0TLX5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 82.
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=ECP_0014;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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}.
DR   EMBL; CP000247; ABG68056.1; -; Genomic_DNA.
DR   RefSeq; WP_000516135.1; NC_008253.1.
DR   SMR; Q0TLX5; -.
DR   PRIDE; Q0TLX5; -.
DR   EnsemblBacteria; ABG68056; ABG68056; ECP_0014.
DR   KEGG; ecp:ECP_0014; -.
DR   eggNOG; ENOG4105CFG; Bacteria.
DR   eggNOG; COG0443; LUCA.
DR   HOGENOM; HOG000228136; -.
DR   KO; K04043; -.
DR   OMA; ISIKRHM; -.
DR   BioCyc; ECOL362663:G1G5S-15-MONOMER; -.
DR   Proteomes; UP000009182; 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   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; Q0TLX5.
DR   SWISS-2DPAGE; Q0TLX5.
KW   Acetylation; ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059555"
FT   MOD_RES         109
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
FT   MOD_RES         245
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
FT   MOD_RES         304
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
FT   MOD_RES         421
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
FT   MOD_RES         556
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule: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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