ID A0A0N8GQT8_9CHLR Unreviewed; 628 AA.
AC A0A0N8GQT8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505};
GN ORFNames=SE15_06065 {ECO:0000313|EMBL:KPL84618.1};
OS Thermanaerothrix daxensis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Thermanaerothrix.
OX NCBI_TaxID=869279 {ECO:0000313|EMBL:KPL84618.1, ECO:0000313|Proteomes:UP000050544};
RN [1] {ECO:0000313|EMBL:KPL84618.1, ECO:0000313|Proteomes:UP000050544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GNS-1 {ECO:0000313|EMBL:KPL84618.1,
RC ECO:0000313|Proteomes:UP000050544};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Thermanaerothrix daxensis DSM 23592.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
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:KPL84618.1}.
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DR EMBL; LGKO01000002; KPL84618.1; -; Genomic_DNA.
DR RefSeq; WP_054521172.1; NZ_LGKO01000002.1.
DR AlphaFoldDB; A0A0N8GQT8; -.
DR STRING; 869279.SE15_06065; -.
DR PATRIC; fig|869279.4.peg.1219; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000050544; Unassembled WGS sequence.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00505; HSP90; 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, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505}; Reference proteome {ECO:0000313|Proteomes:UP000050544};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT REGION 1..333
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 334..549
FT /note="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 550..628
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 628 AA; 72133 MW; BB5D76E53DC58C29 CRC64;
MVESAFDPAH EFQTLNFKAE TQQLLDILIH SLYTERDVFL RELISNASDA LTRMHFILLT
ERDVLDPDAE LAITIVPEPD KRALRIIDTG IGMTADEMIE NLGTIAHSGA RAFIQALKEN
NANPNDIIGQ FGVGFYSAFM VAERIEVISR SYKPQASPAR WISTGRETFN IGPCEKVNRG
TEVILYLKED ASEYTQETRL RQIIKKHSEY IPYPIYLGQD KQPVNRQSAL WRQPPQQVKD
EDYEAFYKQL TLDFQPPLFH LHLVIDAPVQ VFALLFIPAS PERGPLSARN EEGLKLYARK
VLIQEYNRDL LPSFFRFIDG VVDSEDLPLN VSRESVQASR VLAQLKRVIT NRLIEALKNW
AKEKPDEYTT FWQRFGRFIR EGIATDEEYG ELLAPLLRFP TLFKPDQWLS LEDYLLTMPA
RQDKIYYLLS DSLGSALNSP HLEIFRRHRY DVLLMTDPLD PFMMLRLKKY QNIELVNAAS
EELPPPESPS EGQDLSESLL SVEEQTRLIN RFKSVLGEKV ADVRITQRLS ESPARLALQQ
GSPSQEIQRV YRLLQSDYSL PKLVLEINPH HPLIRSLYNL PDNDPLLRLG IEQIYENALL
LEGLHANPGD MVKRTEEILL HALQAKTT
//