ID A0A1G0WJB3_9BACT Unreviewed; 626 AA.
AC A0A1G0WJB3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A2475_13730 {ECO:0000313|EMBL:OGV21491.1};
OS Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV21491.1, ECO:0000313|Proteomes:UP000177327};
RN [1] {ECO:0000313|EMBL:OGV21491.1, ECO:0000313|Proteomes:UP000177327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV21491.1}.
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DR EMBL; MHAY01000064; OGV21491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0WJB3; -.
DR STRING; 1798452.A2475_13730; -.
DR Proteomes; UP000177327; 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; 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_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 SMART; SM00387; HATPase_c; 1.
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}; Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 32..189
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..329
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 541..626
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 72229 MW; BD21C149AE7AF21C CRC64;
MTSDEVKAKN EFEYKAEMKQ LLHLIVHSLY THPEVFLREL ISNSSDALNK IRFRRLTDSN
ILDPDSELKI NIDIDEKENT FSITDTGIGM TKEDLIGRIG TIASSGTLEF FKKMEEENKS
LDANLIGQFG VGFYSVFMVT DEINIETTYA VPNSKTYLWK SFGEDKFTVE EIENKPRGTK
ISFKLKDEYK EFAQPWKVKS ILKKYSNFVD FPVYVNAEKV NIVSALWHRK KEDIKDEELN
DFYTFISNDS TPPMAHLLLN IEGILNFRAL IFIPETAPPS LFQDALEKSL QLYSNRIFIQ
DNCKELIPDY LKFVKGVVDT EELPLNVSRE VTQSSPVITK IKNVLVSKIL AQLEDWAENA
QAKYEKFYNN FGSLLKTGIN ADFTHKVQLI ELLRYETSLR PKGEKVSLKE YVQRMAEGQK
EIYYIMGDHR DLIEMNPNLE YFRKNELEVL YLTDPVDVFT IPYIFEYDKK QLKSIEKADI
DIKKVNKEEK SSDTSNKGLL DYFKEVLGDK VEDVIESNRL VDSAVTLVVG KQGFDPQVEK
MMQYIDKNFT HSKRILEVNT SHNIIRNINS LFIANSNPEL VNNAILQLYE GALLLEGKLP
SPNEFLKRMN EFIELSTKSK NVGEVS
//
