DNAK_DESPS
ID DNAK_DESPS Reviewed; 633 AA.
AC Q6AMQ3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=DP1643;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG36372.1; -; Genomic_DNA.
DR RefSeq; WP_011188884.1; NC_006138.1.
DR AlphaFoldDB; Q6AMQ3; -.
DR SMR; Q6AMQ3; -.
DR STRING; 177439.DP1643; -.
DR EnsemblBacteria; CAG36372; CAG36372; DP1643.
DR KEGG; dps:DP1643; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000602; 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; 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 Reference proteome; Stress response.
FT CHAIN 1..633
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225958"
FT REGION 599..633
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 633 AA; 68122 MW; EE59B302B8A0D341 CRC64;
MGKIIGIDLG TTNSCVSVME GGEPKVIANV EGNRTTPSVV AFADNDERLV GMIAKRQAVT
NPERTVYAAK RLIGRKFTDA EVQRSQEVSP FDIVEGISGS VAIQVEGHKY RPAEISAMVL
GKMKQTAEEY LGEEVTEAVV TVPAYFNDSQ RQATKDAGKI AGLDVKRIIN EPTAASLAYG
LDKKVEEKIA VFDLGGGTFD VSVLEIGDGV FEVKSTNGDT FLGGEDFDMR IVHWLADEFK
REQGIDLRSD KMALQRLKEE AEKAKMELST TVETDINLPF ITADASGPKH LNIKLSRSKF
ETLVEDLVER TVGPCKTALK DAGLSASQID EVILVGGMSR MPMVQKKVVE IFGKEPHKGV
NPDEVVAIGA AIQGGVLQGD VKDVLLLDVT PLSLGIETLG GVTTKLIEKN TTVPTKKSQV
FSTAADNQPA VSIHVLQGER EMAEGNKTIG RFELADIPTA PRGVPQIEVT FDLDANGILN
VSAKDMGTGK EQSIKITASS GLTDEEIDRM TKDAELHADE DKKRKELVEA RNSADGLIHS
TEKTLKDLGD KVDAETKENV EKEIANVKTA LEGDDVEAIK AAIEALTAAS HKLAELMYQQ
ASQETPGDGD AGAAGAKKKD DDDVVDADYE EVK