ID A0A2V2EYD3_9FIRM Unreviewed; 638 AA.
AC A0A2V2EYD3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, 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=DES51_10610 {ECO:0000313|EMBL:PXX78893.1}, DWZ33_03020
GN {ECO:0000313|EMBL:RHN03050.1};
OS Dielma fastidiosa.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dielma.
OX NCBI_TaxID=1034346 {ECO:0000313|EMBL:RHN03050.1, ECO:0000313|Proteomes:UP000284169};
RN [1] {ECO:0000313|EMBL:PXX78893.1, ECO:0000313|Proteomes:UP000247612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC118 {ECO:0000313|EMBL:PXX78893.1,
RC ECO:0000313|Proteomes:UP000247612};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RHN03050.1, ECO:0000313|Proteomes:UP000284169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF31-27BH {ECO:0000313|EMBL:RHN03050.1,
RC ECO:0000313|Proteomes:UP000284169};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RHN03050.1}.
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DR EMBL; QJKH01000006; PXX78893.1; -; Genomic_DNA.
DR EMBL; QRQL01000001; RHN03050.1; -; Genomic_DNA.
DR RefSeq; WP_022937380.1; NZ_QRQL01000001.1.
DR AlphaFoldDB; A0A2V2EYD3; -.
DR STRING; 1034346.GCA_000313565_01066; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000247612; Unassembled WGS sequence.
DR Proteomes; UP000284169; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000247612};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 25..182
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 558..638
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 493..528
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 638 AA; 74005 MW; EB75DB0DB4A91448 CRC64;
MSKKKAFKAE SKRLLDLMIN SIYTHKEIFL RELISNASDA IDKYYYLSLS DENITADRSA
LKIQLSVDKE HRTLTISDNG IGMNKDELEE NLGTIAKSGS LAFKEKMEAE EKNDEDVDII
GQFGVGFYSA FMVASDVVVE SRKAGEEEAY RWESNAVDGY TIDKCEKAEH GTTITLVLKE
DSEDEKYSQY LETYEIENLI KKYSDYIRYP ITMFVSHEEP KEEGSEEMQL VVEEKTLNSM
VPLWKRNKSE ITKEEYNEFY KNKFNDYMDP QKVIHTHVEG SVNFDTLLFI PSKAPYNYYS
NEYEKGLQLY SRGVFIMDKA SELIPEYFRF VRGLVDSQDL SLNISREMLQ HDRQLKAIAS
KIEKKIKSEL VNMLKNDREE YEKFWKNFGL QIKFGIYNDY GMHKEMLQDL LMFTSSHEMK
LTTLDEYVSR MKEGQDVIYY VAGDNLDKLD KLPSAELVKD KGYEILYLTD NVDEFALQVM
MNYQEKNFKN IAQGDLNLES EEEKKEIEEK AEENKDMLSD LKETLKDKVS DVVISTRLKS
HPVCLSAGEG MSFEMEKVLS QMPEGNPYGM KATRILEINP NHPIFEALQK LYGRDKDKVK
DYADLLYDQA LLIEGFDLDD PISFSNKICN LMVDASKE
//
