ID U2P7Z6_9FIRM Unreviewed; 635 AA.
AC U2P7Z6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=HMPREF0367_00422 {ECO:0000313|EMBL:ERK46625.1};
OS Faecalitalea cylindroides ATCC 27803.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalitalea.
OX NCBI_TaxID=649755 {ECO:0000313|EMBL:ERK46625.1, ECO:0000313|Proteomes:UP000016658};
RN [1] {ECO:0000313|EMBL:ERK46625.1, ECO:0000313|Proteomes:UP000016658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27803 {ECO:0000313|EMBL:ERK46625.1,
RC ECO:0000313|Proteomes:UP000016658};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:ERK46625.1}.
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DR EMBL; AWVI01000020; ERK46625.1; -; Genomic_DNA.
DR RefSeq; WP_035400865.1; NZ_KI270978.1.
DR AlphaFoldDB; U2P7Z6; -.
DR PATRIC; fig|649755.3.peg.383; -.
DR HOGENOM; CLU_006684_3_0_9; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000016658; 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 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}; Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 25..178
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..635
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 493..524
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 635 AA; 73765 MW; D7012C6470E34D74 CRC64;
MARKKQFKAE SKRLLDLMIN SIYTHKEIFL RELVSNASDA IDKYYYSNAG HVDPSTFEIR
IEPNKEARTL TISDTGIGMS KEELEENLGT IAKSGSLAFK EQMENNKEHE NDVDIIGQFG
VGFYSAFMVA KELCVISKKD GSDEAYKWIS DGDSGYTIEP AEKETTGTTI ILTLKDDTEN
DDYSKYLETY TLKDLIKKYS DYIRYPIKMN VETSKIKAET KDSDKPEYET VIEDQTLNSM
VPLWKRQKSK ITDEEYNQFY KDHFYDYADP KRVIHFSVEG NVSFTALLYI PSHVPQGFYH
QDYKKGLQLY CRGVFIMDHA EELLPDYLRF VKGLVDSQDL SLNISREMLQ HDHQLKAIAS
RIEKKILSEL TNMLTKERET YEEFWKEFGL NIKFGVYNNY GMDKDKLQDL LLFYSSKDQK
LVTLNEYVNR MKEDQKDIYF VSGSDVNLID KLPIVQTLKK KDYEVLYLTD EVDEFVMQTL
MTYREKTFRN AAQGDLDLDS EEEKQELEKA KEDNKELLKF MKESLHDQVA EVKLSNRLID
DPVCLTAGEG LSFEMEKVFA NMPKDNPMMP MKATRILEIN PNHPIFETLK EAFSSNKDKV
AEIADVLYNQ ALLIEGFKIE DPIAYSRKIC ELLVK
//
