DNAK_THERP
ID DNAK_THERP Reviewed; 633 AA.
AC P96133; B9L0E7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=trd_1640;
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC Thermomicrobium.
OX NCBI_TaxID=309801;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8990285; DOI=10.1128/jb.179.2.345-357.1997;
RA Gupta R.S., Bustard K., Falah M., Singh D.;
RT "Sequencing of heat shock protein 70 (DnaK) homologs from Deinococcus
RT proteolyticus and Thermomicrobium roseum and their integration in a
RT protein-based phylogeny of prokaryotes.";
RL J. Bacteriol. 179:345-357(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U80216; AAB41740.1; -; Genomic_DNA.
DR EMBL; CP001275; ACM06374.1; -; Genomic_DNA.
DR RefSeq; WP_015922585.1; NC_011959.1.
DR AlphaFoldDB; P96133; -.
DR SMR; P96133; -.
DR STRING; 309801.trd_1640; -.
DR EnsemblBacteria; ACM06374; ACM06374; trd_1640.
DR KEGG; tro:trd_1640; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_0; -.
DR OMA; DKMVLQR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000447; 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 Stress response.
FT CHAIN 1..633
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078573"
FT REGION 601..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 29
FT /note="N -> T (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..45
FT /note="PT -> R (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="E -> A (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..109
FT /note="DRW -> ERS (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="L -> R (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..190
FT /note="EEKVA -> RGEGG (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..226
FT /note="DTHLGGDD -> YTHTPLVH (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="R -> A (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..237
FT /note="WLCD -> LALH (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..254
FT /note="MAL -> IV (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 292..294
FT /note="VKT -> TVK (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..302
FT /note="SKLEQ -> ARLQAE (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="R -> A (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..530
FT /note="EL -> DV (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 583..605
FT /note="PAYDELARTLSQVGARMYEQAGA -> GLRRAGADPLPGRRPHVRAGPAP
FT (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="Missing (in Ref. 1; AAB41740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 69521 MW; 488123DF26A9D7A2 CRC64;
MGRVIGIDLG TTNSVMAVIE GGEPVVIPNA EGERLTPSVV AITPTGERLV GRFAKRQAIT
NPENTIYSIK RFMGRRFDDP EVQRTIKLVP YQVRRAQNGG VEVKMGDRWY TPQEISAMIL
QKLKQDAEAY LGETVDKAVI TVPAYFDDSQ RNATKDAGRI AGLEVLRIIN EPTASALAYG
LDKKGEEKVA VYDLGGGTYD ISILDISEGV FQVLATNGDT HLGGDDFDQR IIDWLCDEFK
RETGIDLRQD RMALQRLKEA AEKAKIELSS VQQTEINLPF ITADATGPKH LVKTLTRSKL
EQLVADLVEK TIPPMEQALK DAGLSPRDVD EVVLVGGQTR MPLIQRKVQE FFGKEPHKGI
NPDEVVAIGA AIQAGVLAGE VKEVLLLDVT PLTLAIETLG GVATPIIPRN TTIPTRKSQI
FTTASDNQTQ VEIHVVQGER PMAADNKTLG RFILDGIPPA PRGVPKIEVT FDIDANGILT
VSARDLATGR EQKITITAST GLTEEEIQRM IREAEEHAEE DRRKREAIEL RNQAEALLYQ
AEKTLNEFSD RIPSELKLEL ENKMQAVREI VERDPMNTAR LRPAYDELAR TLSQVGARMY
EQAGATASTG PDGGGRTSGA PGEETVEGEY REV
