DNAK_SHESH
ID DNAK_SHESH Reviewed; 640 AA.
AC A8FYU0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Ssed_3409;
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) 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; CP000821; ABV38013.1; -; Genomic_DNA.
DR RefSeq; WP_012143743.1; NC_009831.1.
DR AlphaFoldDB; A8FYU0; -.
DR SMR; A8FYU0; -.
DR STRING; 425104.Ssed_3409; -.
DR PRIDE; A8FYU0; -.
DR EnsemblBacteria; ABV38013; ABV38013; Ssed_3409.
DR KEGG; sse:Ssed_3409; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002015; 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..640
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079247"
FT REGION 601..640
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 640 AA; 69031 MW; EB106914ADFA591D CRC64;
MGKIIGIDLG TTNSCVAVLD GDTPRVLENA EGDRTTPSII AYTGEEILVG QPAKRQAVTN
PTNTFFAIKR LIGRRFKDDE VQRDVDIMPF KIIGADNGDA WVEAHGKKMA PPQVSAETLK
KMKKTAEDFL GEEVTEAVIT VPAYFNDSQR QATKDAGRIA GLEVKRIINE PTAAALAYGI
DKKQGDNIVA VYDLGGGTFD ISIIEIDSVD GEQTFEVLAT NGDTHLGGED FDNRLINYLA
DEFKKEQSLD LRNDPLAMQR LKEAAEKAKI ELSSASQTEV NLPYITADAT GPKHLVVKIT
RAKLESLVED LITRTLEPLK VALADADLSV SDINEVILVG GQTRMPKVRT EVSEFFGKEL
RQDVNPDEAV AIGAAVQAGV LSGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
ASQTFSTADD NQSAVTIHVL QGERKQSSGN KSLGQFNLEG IEAAPRGMPQ IEVAFDIDAD
GILHVSATDK KTGKAQNITI KASSGLSEEE VEAMVRDAEA HADEDAKFEE LVTARNQADG
MVHATKKQIE EAGEALPSDE KEKIETAMAA VDTAVKGNDK EAIEKSTQEL MEASSKLMEI
AQAKAQAEQG QQAPEGEAQA AKPDEDVVDA EFEEVKDDKK