DNAK_SHEWM
ID DNAK_SHEWM Reviewed; 640 AA.
AC B1KRT2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Swoo_3583;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
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 Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-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; CP000961; ACA87847.1; -; Genomic_DNA.
DR RefSeq; WP_012326180.1; NC_010506.1.
DR AlphaFoldDB; B1KRT2; -.
DR SMR; B1KRT2; -.
DR STRING; 392500.Swoo_3583; -.
DR PRIDE; B1KRT2; -.
DR EnsemblBacteria; ACA87847; ACA87847; Swoo_3583.
DR KEGG; swd:Swoo_3583; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_0_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002168; 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..640
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119758"
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; 68975 MW; E076FB0141B0C2B7 CRC64;
MGKIIGIDLG TTNSCVAVLD GDKARVLENA EGDRTTPSII AYTGEETLVG QPAKRQAVTN
PTNTFFAIKR LIGRRFKDDE VQRDVDIMPF KIIGADNGDA WVEAHDKKMA PPQVSAEILK
KMKKTAEDFL GEEVTEAVIT VPAYFNDSQR QATKDAGRIA GLEVKRIINE PTAAALAYGI
DKKQGDNIVA VYDLGGGTFD ISIIEIDSVD GEQTFEVLAT NGDTHLGGED FDNRLIKYLA
DEFEKEQGMN LRNDPLAMQR LKEAAEKAKI ELSSTTQTEV NLPYITADAS GPKHLVVKVT
RAKLESLVED LVTRTLEPLK VALADADLSV SDVNEVILVG GQTRMPKVRA EVSAFFGKEL
RQDVNPDEAV AIGAAVQAGV LSGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
ASQTFSTADD NQAAVTIHVL QGERKQSSGN KSLGQFNLEG IEPAPRGMPQ IEVAFDIDAD
GILHVSATDK KTGKAQNITI KASSGLSDEE VEAMVRDAEA HADEDAKFEE LVTARNQADG
MVHATKKQIE EAGEALPAED KEKIETAMSA VETAVKGSDK EAIEKSTQEL MEASSKLMEI
AQAKAQAEQG QQAPEGEAQA AKPDEDVVDA EFEEVKDDKK