ID   HTPG_SODGM              Reviewed;         628 AA.
AC   Q2NV58;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 100.
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=SG0692;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE73967.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP008232; BAE73967.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2NV58; -.
DR   SMR; Q2NV58; -.
DR   STRING; 343509.SG0692; -.
DR   PRIDE; Q2NV58; -.
DR   EnsemblBacteria; BAE73967; BAE73967; SG0692.
DR   KEGG; sgl:SG0692; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   Proteomes; UP000001932; 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; Stress response.
FT   CHAIN           1..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000237003"
FT   REGION          1..340
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          341..556
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          557..628
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   628 AA;  71248 MW;  77F4E16F7B012301 CRC64;
     MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSQPDLYEGD
     GELRVRLSCD KEKRTLTFSD NGIGMRREEV IDNLGTIAKS GTKAFLESMG SDQLKDSQLI
     GQFGVGFYSA FIVADKVTVR TRAAGAKPDG GVFWESAGEG DYTIADITKP ERGTEITLHL
     REGEDDFLDD WRLKSVIGKY SDHIVLPVEI ETRSKSEEEG SDEEVVTWEK INKAQALWTR
     NKADISDDEY KEFYKHLSHD FSEPLSWSHN RVEGKQEYTS LLYIPAKAPW DMWNREHKHG
     LKLYVQRVFI MDDAEQFMPN YLRFVKGLID SNDLPLNVSR EILQDSRVTQ NLKGALTKRA
     LSMLEKLAKD DAQQYQSFWQ EFGLVLKEGA GEDPTNGEAV AKLLRFASTH GDSPAQTVSL
     EEYVGRMVEG QEKIYYITAD SYAAAKSSPH LELLRKKGIE VLLFSDRIDE WMMSYLTEFD
     GKAFQSVSKA DPSLDKLADE EDEEQKEVEK ALEPFVERVK TYLGERVKEV RLTHRLTDTP
     AVVTTDADDM TTQMAKLFAA AGQAAPEIKY IFELNPDHAL VKRTANLGDD GAFGDWVELL
     LDQALLAERG TLDDPNQFIR RMNQLLNA