DNAK_MOOTA
ID DNAK_MOOTA Reviewed; 612 AA.
AC Q2RKX4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Moth_0585;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC18915.1; -; Genomic_DNA.
DR RefSeq; WP_011392122.1; NC_007644.1.
DR RefSeq; YP_429458.1; NC_007644.1.
DR AlphaFoldDB; Q2RKX4; -.
DR SMR; Q2RKX4; -.
DR STRING; 264732.Moth_0585; -.
DR EnsemblBacteria; ABC18915; ABC18915; Moth_0585.
DR KEGG; mta:Moth_0585; -.
DR PATRIC; fig|264732.11.peg.629; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
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..612
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059604"
FT REGION 578..612
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 612 AA; 66215 MW; 0795D84F713ED45B CRC64;
MSKVIGIDLG TTNSCVAVME GGEAVVIPNA EGGRTTPSVV AFTKEGERIV GQVAKRQAIT
NPDRTVISIK RHMGTNYKVK IDNKEYTPQE ISAMILQKLK ADAEAYLGEK VTQAVITVPA
YFTDSQRQAT KDAGRIAGLE VLRIINEPTA ASLAYGLDKG EDQTILVYDL GGGTFDVSIL
ELGDGVFEVK ATSGNNRLGG DDFDQRIMDY LVDICRREHG VDLTQDKMAM QRLKEAAEKA
KIELSGMTST NINLPFISAT PNGPVHLDVN LTRAKFEELI ADLVEKTVGP TRQALADAGL
EPKDIDKVLL VGGSTRVPLV QETVRKILGQ EPHKGINPDE CVALGAAIQG GVLAGEVKDV
LLLDVTPLSL GIETLGGVFT KLIERNTTIP TSKSQIFSTA ADNQTTVEIH VLQGERAMAA
DNKTLGRFQL TGIPPAPRGV PQIEVKFDID ANGIVHVSAK DLGTGKQQAI TITSSSGLSE
EEIQRMVKEA EASAEADRRR KEEIETRNQA DSLIYQAERT LKEFKDKADQ NDVDRIEKAK
KELQEVLDSK NNDKIKEKME ALSQALYTLT TKVYQQAGAQ AGAQGQGAAG GQKQDGNVYD
ADYKVVDDDK KE