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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
 
 
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