DNAK_EDWI9
ID DNAK_EDWI9 Reviewed; 635 AA.
AC C5B7L7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=NT01EI_0672;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001600; ACR67894.1; -; Genomic_DNA.
DR RefSeq; WP_015870088.1; NC_012779.2.
DR AlphaFoldDB; C5B7L7; -.
DR SMR; C5B7L7; -.
DR STRING; 67780.B6E78_14020; -.
DR PRIDE; C5B7L7; -.
DR EnsemblBacteria; ACR67894; ACR67894; NT01EI_0672.
DR GeneID; 7962006; -.
DR KEGG; eic:NT01EI_0672; -.
DR PATRIC; fig|634503.3.peg.605; -.
DR HOGENOM; CLU_005965_2_4_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001485; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
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; SSF53067; SSF53067; 2.
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; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..635
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000205186"
FT REGION 603..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 635 AA; 68509 MW; 448374856F3FF5D3 CRC64;
MGKIIGIDLG TTNSCVAVMD GGKARVLENA EGDRTTPSII AYTQDGEVLV GQPAKRQAVT
NPQNTLFAIK RLIGRRFEDA EAQRDKDIMP YKIVAADNGD AWVEVKDQKI APPQISAEVL
KKMKKTAEDF LGETVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
MDKGVGNRTI AVYDLGGGTF DISIIEIDDV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL
VDEFKKEQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
TRAKLESLVE ELVARSMEPL KVALKDAGLS VSDIDDVILV GGQTRMPMVQ KQVADFFGKE
PRKDVNPDEA VAIGAAVQGG VLAGDVKDVL LLDVTPLSLG IETMGGVMTA LISKNTTIPT
KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GIQPAPRGMP QIEVTFDIDA
DGILHVSAKD KNSGREQNIT IKASSGLSED EIKQMVRDAE ANAEADRKFE ELVQVRNQAD
QLVHGTRKLV EEAGDKLPAT DKSAIEEAVK ALEAASKGED KADIEAKIQA LVQSSAKLQE
LAQQQAQAGE AQADTSAKKD DDVVDAEFEE VKDKK