ID A0A1G1IUW3_9BACT Unreviewed; 642 AA.
AC A0A1G1IUW3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 08-NOV-2023, entry version 21.
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=A2Y02_00070 {ECO:0000313|EMBL:OGW72195.1};
OS Omnitrophica bacterium GWA2_52_12.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801816 {ECO:0000313|EMBL:OGW72195.1, ECO:0000313|Proteomes:UP000179888};
RN [1] {ECO:0000313|EMBL:OGW72195.1, ECO:0000313|Proteomes:UP000179888}
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:OGW72195.1}.
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DR EMBL; MHFB01000015; OGW72195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1IUW3; -.
DR Proteomes; UP000179888; 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; 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; 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.
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 DOMAIN 26..202
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..346
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 560..642
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 642 AA; 72127 MW; E11C28467F0CF294 CRC64;
MSKETIEFKA EVSQVLNLVI HSLYSHREVF LRELISNSAD AIDKRRFESL THPEVADASG
AYEIRILPDK DKKTLTIHDN GIGMTRDEVV RNIGTIAASG SRAFLEKLKE NQTVDAPSAK
AGASSSKAGK ASPQAGVELI GQFGVGFYSA FMVAERVEVI TQSAAGGPAV HWESSGEGGY
SIEETTRTGA GTDVILHLRD EAQEFLEEWQ ISSIIQKYSD YVPHPVILEK KGGEKETLNK
VTAIWRRPKS EIKEEEYAEF YKYISHNDDE PLAWTHHTIE GGIEFRLLLF IPKKAPLNLF
REDSHSLRLH VKRMFVTEDL KGLIPVFLRF VKGVVDSEDL PLNVSRETLQ HNALIPKMQK
QITKKVIEML EDLAKNEPEK YKAFFKEFGA ALKEGLGGAF DYRERLVELM RYPSTAVAES
DRTSLSDYVS RMKGGQKEIY FIAGPSREAC ERSPHLEALK SRGLEVLLMS DVIDDWTIPY
IESYKGSKLR SVMKGDLDLS FIEGAPAKEE APAEVKPLLD KIRAVLQEEV KDVRVTQRLA
DSPCCLVADE GDMDAHMERI MKAMHQETPL AKRILEINPK HALIQNLKAL VEKNPQDARF
GFWVRLLYNQ AQIAEGSELR KPEDFLRGVT ELLTEASGDA VK
//