DNAK_DESHD
ID DNAK_DESHD Reviewed; 614 AA.
AC B8FUN4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=Dhaf_4299;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL22304.1; -; Genomic_DNA.
DR RefSeq; WP_005816476.1; NC_011830.1.
DR AlphaFoldDB; B8FUN4; -.
DR SMR; B8FUN4; -.
DR PRIDE; B8FUN4; -.
DR EnsemblBacteria; ACL22304; ACL22304; Dhaf_4299.
DR KEGG; dhd:Dhaf_4299; -.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000007726; 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; 2.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 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..614
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133143"
FT REGION 576..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 614 AA; 65638 MW; 52BDE684FF181D0A CRC64;
MGKVIGIDLG TTNSCVAVME GGEAVVITNA EGNRTTPSVV GFSKTGERLA GQVAKRQAVS
NPDKTVISIK RHMGTDYKVK IDDKSYSPQE ISAMILQKLK ADAEAYLGQT VTEAVITVPA
YFTDAQRQAT KDAGTIAGLD VKRIINEPTA AALAYGLDKQ EDQTVLVFDL GGGTFDVSLL
ELSQGMVEVK ATSGNNKLGG DDFDQRLIDY MVAEFKKDQG VDLAKDRVAL QRLKEAAEKA
KVELSGVSTT NVNLPFITMT GEGPAHLDMN ITRAKFEELT ADLVEATLGP TRQALADAKL
SWNEVNQVIL VGGSTRIPAV QEAIKKLSGK EPHKGVNPDE VVALGAAIQG GVLAGEVKDI
ILVDVTPLSL GIETLGGVFT RIIDRNTTVP TTKSQVFSTA ADSQTSVDIH VLQGEREMAA
YNKTLGRFQL SGIPPAPRGI PQIEVKFDID ANGIVHVSAK DMATGNEQKV TITASTGLSQ
EEIEKMKKDA EAHADEDKKR KELIDAKNQA DSMVYQTEKT LKDFEGKIPD NEAEPIKKAL
EELKTAAAGE NIELIKEKTE GVTKVLYPII EKMYQQTGGA APGPDMGADP GAGGAQGDDN
VVDAEYTEVD KDQK
