ID   HTPG_RUTMC              Reviewed;         616 AA.
AC   A1AWE2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Rmag_0493;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthia.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(2007).
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; CP000488; ABL02249.1; -; Genomic_DNA.
DR   RefSeq; WP_011737874.1; NC_008610.1.
DR   AlphaFoldDB; A1AWE2; -.
DR   SMR; A1AWE2; -.
DR   STRING; 413404.Rmag_0493; -.
DR   EnsemblBacteria; ABL02249; ABL02249; Rmag_0493.
DR   KEGG; rma:Rmag_0493; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002587; 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..616
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014949"
FT   REGION          1..334
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          335..549
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          550..616
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   616 AA;  70284 MW;  1282A4A5D41456C0 CRC64;
     MAEKQIHTFQ TEVSQLLDLM IHSLYSNKEI FLRELVSNSS DAVDKLKFKS LSDDTLIEGK
     EELQIHINTN KDASTITITD NGIGMTEAEV NKNIGTIANS GTKKFLKSLD EKQTKDSNLI
     GQFGVGFYSS FIVADKVELI TRKAGSKSKK GTKWTSTGKG KYSIERVNCL NFGTSVTLHI
     KKDEKEFLDD YRLRGIISKY SDHITVPIMM IKASEDGKDI EYERINKANA FWSQDKRDLK
     QENYDEFYKS LTYDFEAPLT QLHNRVEGNI DYTSLLFIPS KAPHDMWEPK RKGGIKLYAK
     RVFIMEDNEA LMPLYLRFVK GVIDTADLPL NVSREILQGN KVVDTIRKAS VSRVLKELEK
     MAKNKPEDYE KFWQEFGMVM KEGVVEDFAN KDKIAKLLRF TTNKSESAAQ TATLECYVKS
     MQKDQKAIYY ITAETYEAAK GSPHLEIFNQ KDIEVLLLSD RVDEWMVNNF GKFEDVPLKS
     ITKGDLEGLD SKEEKKAKEE VSKNFEKVIE KMQKILDTQV KEIKVSSRLS DSPSCLVVDE
     NEMGGNMERI MKSLGQDVPD TKPILEINPN HPLVKKLKTK IDEDLVKVLF DQAVLSEGVQ
     LKDPAEFVKR INKLIN