ID   HTPG_TREPA              Reviewed;         639 AA.
AC   O83949;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 124.
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=TP_0984;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65938.1; -; Genomic_DNA.
DR   PIR; F71258; F71258.
DR   RefSeq; WP_010882428.1; NC_021490.2.
DR   AlphaFoldDB; O83949; -.
DR   SMR; O83949; -.
DR   IntAct; O83949; 10.
DR   STRING; 243276.TPANIC_0984; -.
DR   EnsemblBacteria; AAC65938; AAC65938; TP_0984.
DR   KEGG; tpa:TP_0984; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_12; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000811; 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; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..639
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063018"
FT   REGION          1..348
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          349..565
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          566..639
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   639 AA;  72938 MW;  3E8FDBAC2282C31D CRC64;
     MAQYEFQTEV SQLLTLIIHS LYSHKEIFLR ELISNASDAL DKLKYEALVD GTYKQLHCEA
     RIDIAFEEDA QRLVVRDTGI GMNAEDLRAN LGTIARSGTK AFLSTLTRDQ KQDSNLIGQF
     GVGFYSAFMV ASKVEVITKK AAENTVWKWT SEGQNAYTLD EVDAAAFPVL EGVAEGSAGT
     CVVLHLSQEN SEFATRWRLE EVIKKYSDHI AFPIYLHYLQ KEYDKDGAVT DTQKKVDQVN
     DAGALWKRPK SELKEEDYHR FYQTLTRDST PPLLYVHTKA EGTQEYVTLF YVPAKAPFDL
     FHADYKPGVK LFVKRVFITD DEKELLPVYL RFVRGVIDSE DLPLNVSREI LQQNRVLAAI
     KSASVKKLLG EFKRLAECDG KKYDEFITQY NRPLKEGLYS DYEHREQLLE LVRFRTLSES
     VPEDGWTSFA EYVSRMKPDQ KAIYYIAGND DRVLRQSPHA ESYRLQGFEV LVMSDDIDGI
     VMPSVSKYKE WELRAINRLG SEEELRPNEE TDAAAQREQG FKPLLERLTH ILSDSVKEVR
     LSKRLSDSVS CIVIDENDPT VQMERLMRAT GQTHKSKIKP ILEINASHTL VQKLKESTDE
     AFVEDLAFVL LDQALLIEGM DVGSSVDFVK RVNRLLARG