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 27-MAR-2024, entry version 132.
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; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC 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.TP_0984; -.
DR EnsemblBacteria; AAC65938; AAC65938; TP_0984.
DR KEGG; tpa:TP_0984; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_12; -.
DR OrthoDB; 9802640at2; -.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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
//
