ID A0A2I1M8W1_9FIRM Unreviewed; 613 AA.
AC A0A2I1M8W1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CYJ34_05075 {ECO:0000313|EMBL:PKZ16573.1};
OS Anaerococcus octavius.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=54007 {ECO:0000313|EMBL:PKZ16573.1, ECO:0000313|Proteomes:UP000234335};
RN [1] {ECO:0000313|EMBL:PKZ16573.1, ECO:0000313|Proteomes:UP000234335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0119 {ECO:0000313|EMBL:PKZ16573.1,
RC ECO:0000313|Proteomes:UP000234335};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:PKZ16573.1}.
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DR EMBL; PKGS01000003; PKZ16573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1M8W1; -.
DR Proteomes; UP000234335; 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; 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_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; 2.
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.
DR PROSITE; PS00298; HSP90; 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}; Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT REGION 1..342
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 543..613
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 613 AA; 70852 MW; 3D09EC8C16A3E83C CRC64;
MKQEFKAEAQ KVMDLMINSI YTNKEIFLRE LISNASDALD KLYYKDLKSD SETNKDDYYI
QIIPDRENRT LTIKDTGIGM DENELVENLG TIAKSGTDSF KKSVENSDIK DLIGQFGVGF
YSAFMVADKV IVKTKKYGSD TGYIWESENA DGFEISETDQ EDNGTAITLF LKENTEDENF
DEYLDQFKIK NLVNKYSNYI RYPIKMEVTK TRLAEDSTQE DPKYEDYKEL DVLNSETPIW
KKNKSDLADE DYINFYQDQH FGFDEPLSWI HFKVEGAVQF KALIYIPKKA PFDYYSKDYQ
KGLQLYTHGV KIMERSEDLL HDAYSFAKGV VESDDLTLNI SRETLQQDRQ LRVISKQINK
KINKHLLDLQ KNEPEKYSEF FKEFGNNIKV AIYEAYGSNK EELQNLLLFH SKNEDKLISL
REYKENAKSS EENILYATGD SLEKIKNSPA LAMVDEDSDV LLLDEAIDEF LIKMLEEYDG
LSFKSLAEED DSEVENEDQK DLVGKLLENL PDDVVDIKFN EKMGDIPAMI KQRGDISIEM
EKALKNNPQG PAIKAEKVLE INKNSKAYEL LENAKDDENK NEIVNLLLDQ AKLIEGLEIE
DPVSYTKNIW KLI
//
