ID DNAK_THISH Reviewed; 641 AA.
AC B8GNX1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=Tgr7_0972;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL72060.1; -; Genomic_DNA.
DR RefSeq; WP_012637544.1; NC_011901.1.
DR AlphaFoldDB; B8GNX1; -.
DR SMR; B8GNX1; -.
DR STRING; 396588.Tgr7_0972; -.
DR KEGG; tgr:Tgr7_0972; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000002383; 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 CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375:SF541; CHAPERONE PROTEIN DNAK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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..641
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133169"
FT REGION 577..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 641 AA; 69312 MW; F0801F1E9D682930 CRC64;
MGKIIGIDLG TTNSCVAVME GDKAKVIENA EGARTTPSIV AFTEDGEVLV GQAAKRQAVT
NPKNTLFAVK RLIGRRFEEP EVQKDIKLVP YEIFKADNGD AWVRVRDKKM APPEISARVL
QKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
LDKKRGDSKV AVYDLGGGTF DVSIIEIAEV DGEHQFEVLA TNGDTFLGGE DFDMRLIDYL
VEEFKKEQGI DLKGDPLAMQ RLKESAEKAK IELSSSQQTD VNLPYITADA SGPKHMNIKV
TRAKLESLVE ELIKRTIEPC KVALKDAGLS VSDIDDVILV GGQTRMPKVQ DAVKNFFGKE
PRKDVNPDEA VAVGAAIQAG VLGGEVKDVL LLDVTPLSLG IETLGGVMTK LIEKNTTIPT
KATQVFSTAD DNQTAVTVHV LQGEREMASA NKSLGRFDLT DIPPAPRGVP QVEVMFDIDA
NGILNVSAKD KATGKQQSIV IKASSGLSDE EVERMVRDAE AHADEDKRFH ELVAARNQAD
NLVHATEKSL KELGDQVEAG EKQAIESALS ELREAMKGDN KDEIETRTQK LAEASGKLAE
RVYAKQSAEG GAGEGAGAEQ ASAQQDDVVD AEFEEVDDKK K
//
