DNAK_SHEHH
ID DNAK_SHEHH Reviewed; 638 AA.
AC B0TQC2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Shal_3167;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) 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; CP000931; ABZ77714.1; -; Genomic_DNA.
DR RefSeq; WP_012278237.1; NC_010334.1.
DR AlphaFoldDB; B0TQC2; -.
DR SMR; B0TQC2; -.
DR STRING; 458817.Shal_3167; -.
DR PRIDE; B0TQC2; -.
DR EnsemblBacteria; ABZ77714; ABZ77714; Shal_3167.
DR KEGG; shl:Shal_3167; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001317; 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 Stress response.
FT CHAIN 1..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079245"
FT REGION 601..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 638 AA; 68895 MW; 8A3BC679479D061E CRC64;
MGRIIGIDLG TTNSCVAVLD GGKARVLENA EGDRTTPSII AYTADETLVG QSAKRQAVTN
PTNTVYAIKR LIGRRFKDDE VQRDVDIMPF KIISADNGDA WVEAQGKKMA PPQISAEILK
KMKKTAEDFL GEEVTEAVIT VPAYFNDSQR QATKDAGRIA GLEVKRIINE PTAAALAYGI
DKKQGDNIVA VYDLGGGTFD ISIIEIDSVD GEQTFEVLAT NGDTHLGGED FDNRMIKYLA
DEFKKEQGLD LRNDPLAMQR LKEAAEKAKI ELSSTTQTEV NLPYITADAT GPKHLVVKIT
RAKLESLVED LIKRSLEPLK VALADADLSV SDINEVILVG GQTRMPKVRE EVSAFFGKEL
RQDVNPDEAV AIGAAVQAGV LSGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
ASQTFSTADD NQSAVTIHVL QGERKQSSGN KSLGQFNLEG IEAAPRGMPQ IEVAFDIDAD
GILHVSATDK KTGKAQNITI KASSGLSDEE VEAMIRDAEA HADEDAKFEE LVKSRNQADG
MVHATKKQIE EAGEALPADE KEKIEAAMAN VETAVKGNDK EAIEKSTQEL MEASSKLMEI
AQAKAQAEQG QPEGEAKSAK PEDDVVDAEF EEVKDDKK