ID   HTPG_CHLPM              Reviewed;         625 AA.
AC   A4SEX9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Cvib_1024;
OS   Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS   vibrioformis (strain DSM 265)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 265 / 1930;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA   Schuster S.C., Bryant D.A., Richardson P.;
RT   "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000607; ABP37038.1; -; Genomic_DNA.
DR   RefSeq; WP_011890262.1; NC_009337.1.
DR   AlphaFoldDB; A4SEX9; -.
DR   SMR; A4SEX9; -.
DR   STRING; 290318.Cvib_1024; -.
DR   EnsemblBacteria; ABP37038; ABP37038; Cvib_1024.
DR   KEGG; pvi:Cvib_1024; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_1_10; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
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; Stress response.
FT   CHAIN           1..625
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081521"
FT   REGION          1..332
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          333..545
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          546..625
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   625 AA;  70449 MW;  79C556293301F100 CRC64;
     MSKKTNAPVQ EFEYKAEMKQ LLDLIVHSLY THPEIFLREL VSNAADALSK ARFSSLTDGG
     LMAAAGEDAI HITLDKEKLL FVIEDSGIGM SEDELIANLG TVAKSGTLGF MQSLQEQKKE
     LDGNLIGQFG VGFYSVFMVT ENVTVETRSA QEGSEGLRWQ SSGQGTYTIE KVEKKERGTR
     ISFTLKEEYK EFAEEYRVEQ VIKKYSNFVD FPIYLGEKQL NSVTALWQRP KSELQEGDVH
     EFYKFISNDF EDPLDYLSVS VEGAVSFKAL LFLPQNAPME LLYRQGELEN KGPQLYVKKV
     MIQNECRDLL PEYLRFIAGV VDTEDLSLNV SREVVQSSPV MAKIRQILTT KILGWFEELA
     VEQPEKFKTF YKAFGPIVKI GLNTDFTNRD KLIELLRFES TKTGEGEFVT LKEYVARMGG
     EQKEIYYHSG AGRAQLLANP NLEYFQSRGI EVLLLSDPVD VFVIPSIHEY DSKQLKSIEK
     ADIDFSKEKT EGEEPVAENL LVPLLAKFRE ALGEDIADVV ESHRLVSSPV TIVGGKDAMD
     SQMERMMKMM QQEMPAAKKV LEVNPRHPII RNLSGMMIAN ADNPLINSAI RQLYEGALLL
     EGDLSSTTGF VQRMNELIEA ATLSR