ID   HTPG_TREDE              Reviewed;         640 AA.
AC   P61188;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=TDE_2480;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12997.1; -; Genomic_DNA.
DR   RefSeq; NP_973078.1; NC_002967.9.
DR   RefSeq; WP_010957241.1; NC_002967.9.
DR   AlphaFoldDB; P61188; -.
DR   SMR; P61188; -.
DR   STRING; 243275.TDE_2480; -.
DR   EnsemblBacteria; AAS12997; AAS12997; TDE_2480.
DR   GeneID; 2741453; -.
DR   KEGG; tde:TDE_2480; -.
DR   PATRIC; fig|243275.7.peg.2346; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_12; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000008212; 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; 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   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..640
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063017"
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..640
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   640 AA;  73496 MW;  98DB8F6CFEDC17BD CRC64;
     MAQYKFETEV NQLLSLIIHS LYSNKEIFLR ELVSNASDAL DKLKYLTLSD EAYKQIKFEP
     RIDICFDDTA NTLTVRDTGL GMNEEDLKNN LGTIARSGTK AFLDQLAAAD KKDSNLIGQF
     GVGFYSAFMA ASTIDVISKK AGENDVWKWT SDGKGAYDLE KVDDTAFPII DGVPEGANGT
     CVILHLNNED SEYATRWRIE EIIKTYSDHI AFPIYLHFTE KQYDDKGKVK SEASKTEQIN
     DAGAIWQKPK SELKEEDYFN FYKSLSHDSQ EPLLYVHTKA EGTQEYTTLF YVPSKAPFDM
     FHADYRPGVK LFVKRVFITD DEKELLPTYL RFVRGVIDSE DLPLNVSREI LQQNRILSNI
     KNASVKKLLG EFKKLAENDK EKYNKFIAEF NRPLKEGLYS DYEHREELAD LVRFKTTSPE
     VKEDEWTSFA DYVSRMKSDQ KAIYYITGED EKTLRQSPHL EVYKQKGFEV LIMPDEIDDI
     IIPSLGKYKD WELKAANRAG SDKELNTEEE TKEAEKKEKD FKPVLEKIKE VLGDKVKEVR
     FSKRLSDSPS CIVVDETDPS LQMERMMRAM GQFNTSAVKP ILEVNADHPL VQKLKDSKDK
     EFVEDMSNLL LEQALLVESG ELKAPVDFVK RLNRLMTNLK