ID A0A1H3XWL5_9BACT Unreviewed; 686 AA.
AC A0A1H3XWL5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SEA03859.1};
GN ORFNames=SAMN05444145_101363 {ECO:0000313|EMBL:SEA03859.1};
OS Alistipes timonensis JC136.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1033731 {ECO:0000313|EMBL:SEA03859.1, ECO:0000313|Proteomes:UP000183253};
RN [1] {ECO:0000313|EMBL:SEA03859.1, ECO:0000313|Proteomes:UP000183253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25383 {ECO:0000313|EMBL:SEA03859.1,
RC ECO:0000313|Proteomes:UP000183253};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; FNRI01000001; SEA03859.1; -; Genomic_DNA.
DR RefSeq; WP_010259711.1; NZ_FNRI01000001.1.
DR AlphaFoldDB; A0A1H3XWL5; -.
DR STRING; 1033731.SAMN05444145_101363; -.
DR GeneID; 78308986; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000183253; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000183253}.
SQ SEQUENCE 686 AA; 78853 MW; 5CFB971C33F7F48E CRC64;
MKNGKIGVTT ENIFPVIKKF LYSEHEIFLR ELISNAVDAT QKLKTLSSIG EMKGDLGDLT
IHVAVDKEKK TLTVTDRGVG MTAEEVDKYI NQIAFSGAEE FMEKYKNQAI IGHFGLGFYS
AFMVSDKVEI FTKSFREGAK AVHWSCTGTP EFEMEETDEA RDRGTTIVLH ISEDALEYAE
ESKIEGLLKK YCRFLPIPIA FGKVKEWKDG KYVDTDKDNI INNIEPLWTR KPADITEEQY
KEFYHELYPM GDEPLFSIHL NIDYPFHLTG ILYFPKIRNN FEIQKNKIQL YSNQVYVTDQ
VEGIVPEYLT LLHGVIDSPD IPLNVSRSYL QSDSNVKKIS SYITRKVADR LQELFTTMRA
DYESKWDDLK VFIQYGILTD EKFAEKATGF MLWKNTEGQY FTPKEYTEKV KENQTDKNKT
VVFLYVDDPV AKYTSLEAAK GKGYDVLVMD GQLDNHYINW YESKEKETCF VRVDSDVVDK
LIQKEENVKM SLSEAQQEVL EPVFESQMPK DDKIHYNISF EAMSPDEAPV VITQNEFMRR
MKEMAAMGGG GMSQFYGQMP DNFTIAVNGN HPIVIDILAD VEKAYGDKLR TVTKKIDAAV
AEEKRFDEVV KGKKEEELTP EEKSTREELS KKIVTLRDER NERLREIGGE NRLVKQIIDL
ALLTNGMLKG KNLTDFIQRS ISLIEK
//
