ID D6EAI0_9ACTN Unreviewed; 641 AA.
AC D6EAI0;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 08-NOV-2023, entry version 71.
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=GPA_26660 {ECO:0000313|EMBL:CBL04727.1};
OS Gordonibacter pamelaeae 7-10-1-b.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL04727.1, ECO:0000313|Proteomes:UP000008805};
RN [1] {ECO:0000313|EMBL:CBL04727.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL04727.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929047; CBL04727.1; -; Genomic_DNA.
DR RefSeq; WP_015540071.1; NC_021021.1.
DR AlphaFoldDB; D6EAI0; -.
DR KEGG; gpa:GPA_26660; -.
DR PATRIC; fig|657308.3.peg.2143; -.
DR HOGENOM; CLU_006684_3_0_11; -.
DR BioCyc; GPAM657308:GPA_RS12405-MONOMER; -.
DR Proteomes; UP000008805; Chromosome.
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; 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 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:UP000008805};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT REGION 1..348
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 567..641
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 509..536
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 641 AA; 72315 MW; 650FE57E146E2D8F CRC64;
MRKFKTESKK LLDLMINSIY TNREIFLREL ISNASDAVDK LYFKSLTDKS IELSKDELAI
QVSFDKDART VTVSDSGIGM TKDELDRNLG TIAHSDSMAF KMENDEVQGD DVDIIGQFGV
GFYSSFMVGK SVRVVSKAYG SDEAWAWESD GVEGYTIEPA ERAEHGTDVI ITLKDNTDED
SYDGYLSEYG LKDLVKRYSN YVRYPIRMEV TKSRELPKPE DAGDDYVPQF ENYQELDTVN
SMIPIWKRRK SEVDQEEYNE FYKTDFHDFA DPARTISVHA EGALSYDALL FVPSRAPFDL
YSRDYQKGLA LYSSNVLIME KCEELLPDYY NFVHGVVDSQ DLQLNISRET LQHNSQLRAI
AKKIEKKITS DLEDMRDNDR EGYEAFFENF GRGLKYGIYA SYGSQKDTLA DLLLYYSAKQ
DKLVTLAEYF EAMPEDQPAI YYAAGDSVER LNKMPIVKTV LGKGYDVLLC TQDVDEFCFT
AMRDYGANED GEGAKELKNV ASGDLDFATE DEKKEAEEAT KENEDLFKAL KDALGNEVTK
VAVSARLTDA PACVTTEGPV SLEMERVLSK GPEGPDGVKS QRVLELNAKH PVFDTLKAAH
EAGDNDKIRL YADLLYNQAL LVEGMPIDDP VAFAQNVAKL M
//
