HTPG_YERE8
ID HTPG_YERE8 Reviewed; 624 AA.
AC A1JNB3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=YE3090;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR EMBL; AM286415; CAL13125.1; -; Genomic_DNA.
DR RefSeq; WP_011816876.1; NC_008800.1.
DR RefSeq; YP_001007272.1; NC_008800.1.
DR AlphaFoldDB; A1JNB3; -.
DR SMR; A1JNB3; -.
DR STRING; 393305.YE3090; -.
DR PRIDE; A1JNB3; -.
DR EnsemblBacteria; CAL13125; CAL13125; YE3090.
DR KEGG; yen:YE3090; -.
DR PATRIC; fig|393305.7.peg.3288; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000000642; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT CHAIN 1..624
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014965"
FT REGION 1..336
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 337..552
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 553..624
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 624 AA; 71025 MW; B3C0DCCEB4A81F8C CRC64;
MSMKGQETRG FQSEVKQLLH LMIHSLYSNK EIFLRELISN ASDAADKLRF RALSHPELFE
GDGELRVRLS FDKEKRTLTL SDNGIGMSRE EVIDNLGTIA KSGTKAFLES IGSDQAKDSQ
LIGQFGVGFY SAFIVADKVT VRTRAAGAPA DAGVFWESAG EGDYTIADIT KEDRGTEITL
HLREGEDEYL DNWRLRSVIS KYSDHIALPV EIESKNEEDG TVTWEKINKA QALWTRGKAE
ITDDEYKAFY KHIAHDFTDP LIWSHNRVEG KQEYTSLLYI PAQAPWDMWN RDHKHGLKLY
VQRVFIMDDA EQFMPNYLRF VRGLIDSNDL PLNVSREILQ DSRVTQNLRS ALTKRVLQML
EKLAKDDAEK YQQFWQQFGM ALKEGPAEDG SNKDTIAKLL RFASTHTDSS AQTVSLEDYV
SRMAEGQEKI YYITADSYAA AKNSPHLELF RKKGIEVLLL SDRIDEWMMS YLTEFDGKAF
QSVSKADDSL NKLADEERPE QQEADKALEP FVERVKTLLG ERVKDVRLTH RLTDTPAIVT
TDADEMSTQM AKLFAAAGQQ APEVKYIFEL NPEHSLVKRA ADVADDTQFA EWVELLLDQA
LLAERGTLED PNQFIRRMNQ LLTA