ID   A0A1Q3RP70_9FIRM        Unreviewed;       625 AA.
AC   A0A1Q3RP70;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:OJV65959.1};
GN   ORFNames=BGO41_08480 {ECO:0000313|EMBL:OJV65959.1};
OS   Clostridiales bacterium 38-18.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1895746 {ECO:0000313|EMBL:OJV65959.1, ECO:0000313|Proteomes:UP000185881};
RN   [1] {ECO:0000313|EMBL:OJV65959.1, ECO:0000313|Proteomes:UP000185881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=38-18 {ECO:0000313|EMBL:OJV65959.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJV65959.1}.
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DR   EMBL; MKTL01000002; OJV65959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3RP70; -.
DR   STRING; 1895746.BGO41_08480; -.
DR   Proteomes; UP000185881; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   625 AA;  71789 MW;  BB47FCE99A5252EF CRC64;
     MSKEKGSLSI HSENIFPIIK KWLYSDHDIF VRELISNASD AITKLKQLAS MNEISLSTST
     GYKIDVILDE AAKTITFSDN GIGMTDEEIK KYINQIAFSG AEDFIAQYKD KSDKDQIIGH
     FGLGFYSAFM VAEHVEIHTL SYKEGAKPAL WRCDGGTEFE LEAGTRQDRG TEITLYIGEE
     GISFLNEYTL KSTIKKYCSF MPYEIFLTVI GKEPEKDQDG NAIIEEPKAL NTTQPLYTKS
     PSDCSDEDYK AFYRNTFNDF KEPLFWIHLN MDYPFNLKGI LYFPKLNTEF DTIEGQIKLY
     NSQVFVADNI KEVIPEFLLL LKGVIDCPDL PLNVSRSFLQ NDGFVKKISN YISKKVADKL
     VGLSKTEKET FEGFWEDISP FIKFGGLKDE KFYDLVKDIY LYKTLDNTFK TLDEYLESIK
     EKHENKVFYV SDPIQQAQYI KLFKDHDLDA VILSHGIDSA FISMLESKRE GVSFSRIDAD
     LNEHLTEASD TEDDKKVEKQ EALKTLFEKS LHLENMKLKL ENMKTDSVAS MVVLSEESRR
     MQDMMRMYGM QGLDPNMFKT ETTLILNQKH PLVKHLQDDS IADEALKEMI CQQLYDLAMI
     SHSPLSPEAM TLFIERSQKL MLKLI
//