ID   HTPG_CHLTE              Reviewed;         629 AA.
AC   Q8KE61;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=CT0829;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM72065.1; -; Genomic_DNA.
DR   RefSeq; NP_661723.1; NC_002932.3.
DR   RefSeq; WP_010932510.1; NC_002932.3.
DR   AlphaFoldDB; Q8KE61; -.
DR   SMR; Q8KE61; -.
DR   STRING; 194439.CT0829; -.
DR   EnsemblBacteria; AAM72065; AAM72065; CT0829.
DR   KEGG; cte:CT0829; -.
DR   PATRIC; fig|194439.7.peg.753; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_10; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001007; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..629
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062979"
FT   REGION          1..335
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          336..547
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          548..629
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   629 AA;  71037 MW;  65D57227B6C94CE3 CRC64;
     MSSNPTSSVR EFEYKAEMKQ LLNLIVHSLY THPEIFLREL ISNASDALGK ARFRMLSSDE
     GLDKSGDLKI TITVDKESGS FVIEDTGIGM SEEELISNLG TVASSGTLGF MEALKEQQKE
     GQRLDANLIG QFGVGFYSVF MVTDEVTVET KSIESGLQGW RWKSSGQGSY TIEPVEREAR
     GTRISFILKE EFREFAQEYR VEQIIKKYSN FVEYPIYIGS RQINSMTALW QRPKSELKQE
     EVNEFYKFIA NDFKDPLDYL HVSVEGAVSF KALLFIPSEA PMELLYNQGA LEKRGPQLYV
     KKVLIQHECR DLLPEYLRFV SGVVDTEDLP LNVSRELVQA SPVMAKIKQI LTTKLLGWFD
     TIAKEEPEKF RAFYKAFGTI LKIGLNTDFT NRDKLIDLLR FETTKTVEGE YVTLKEYVGR
     MAEGQTEIYY HSGSSRAQML AHPNLEYFRK RDIEVLLLSD PVDVFVIPSI FEYDKKPLKS
     IEKAEIDMST VEPEGERLSA EGTVGVISLF KEVLGERVAD VVESRRLVSS PVTLVSGKDA
     LDSQFEKMMK MMNKDADMPS TKKILEINTA HPIIRNLAGK HAVGLSTDPV VRAAVTQLFE
     SALLLEGDLE SVADYVSRMN ELVEAATRS