ID   HTPG_BAUCH              Reviewed;         631 AA.
AC   Q1LTX6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=BCI_0117;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA   Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT   sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14114.1; -; Genomic_DNA.
DR   RefSeq; WP_011520321.1; NC_007984.1.
DR   AlphaFoldDB; Q1LTX6; -.
DR   SMR; Q1LTX6; -.
DR   STRING; 374463.BCI_0117; -.
DR   EnsemblBacteria; ABF14114; ABF14114; BCI_0117.
DR   KEGG; bci:BCI_0117; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002427; 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; 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.
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..631
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258503"
FT   REGION          1..338
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          339..554
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          555..631
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   631 AA;  72636 MW;  013BF2EEEC67F83C CRC64;
     MILKEQETLG FQSEVKQLLN LMIHSLYSNK EIFLRELISN ASDAADKLRF LALAKPDLYE
     GNGELYVRII CNKEKRTITI IDNGIGMCRT EVIDNLGTIA KSGTKAFLET IDVKNSKNNQ
     LIGQFGVGFY SAFIVAQKVI VRTRAAGASA DEGVHWESTG EGDYIIAAIN KPERGTEITL
     FLREGEDEFL DDWRIKNTIG KYSDHITLPI EIATNSENKN NNIITWEQIN KAQALWTRNK
     VDVSDQEYKD FYKHLYHDSN DPISWSHNRV EGQQEYTSLL YIPASASWGI WNRDHKYGLK
     LYIKRVLIMD HADYFLPNYL RFVKGIIDCN DLPLNISREM LQHNRITQNL KNAITKRILS
     MLEKLATQNN EQYQNFWQHF GLVIKEGLAE DPNNSKSIAR LLRFSTTHSK SMEQNVSLDE
     YVSRIAEQQE KIYYIIADSY AAANSSPHLE LLQKKGIEVL LLHERIDAWM MNYLIEFNGK
     SFQLVSKADL KLDKFLNENT TEQKDMTKAF EPFIERVKKY LGDRIKEVRL TYSLTDTPAI
     VTIDSNNMTT HMAKLIVASG QNKPDIKYIF ELNPLHPIVK KVSNTDNDIY FSEVIELLLD
     QALLVECGTL ENPNQFVRRI NKLLNHDTIV N