ID A0A1H5TWJ3_9RHOO Unreviewed; 643 AA.
AC A0A1H5TWJ3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=SAMN05216242_103232 {ECO:0000313|EMBL:SEF67153.1}, Tchl_3190
GN {ECO:0000313|EMBL:APR05997.1};
OS Thauera chlorobenzoica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=96773 {ECO:0000313|EMBL:APR05997.1, ECO:0000313|Proteomes:UP000185739};
RN [1] {ECO:0000313|EMBL:SEF67153.1, ECO:0000313|Proteomes:UP000236741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB-1 {ECO:0000313|EMBL:SEF67153.1,
RC ECO:0000313|Proteomes:UP000236741};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APR05997.1, ECO:0000313|Proteomes:UP000185739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB1 {ECO:0000313|EMBL:APR05997.1,
RC ECO:0000313|Proteomes:UP000185739};
RA Goris T., Mergelsberg M., Boll M.;
RT "Complete genome sequence of Thauera chlorobenzoica, a Betaproteobacterium
RT degrading haloaromatics anaerobically to CO2 and halides.";
RL Submitted (DEC-2016) 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; CP018839; APR05997.1; -; Genomic_DNA.
DR EMBL; FNVJ01000003; SEF67153.1; -; Genomic_DNA.
DR RefSeq; WP_075149251.1; NZ_FNVJ01000003.1.
DR AlphaFoldDB; A0A1H5TWJ3; -.
DR STRING; 96773.Tchl_3190; -.
DR KEGG; tcl:Tchl_3190; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000185739; Chromosome.
DR Proteomes; UP000236741; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 31..192
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..348
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 570..643
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 506..538
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 643 AA; 71784 MW; B22E4859F65D8FB5 CRC64;
MSETAAAAQT LNFQAEVKQL LHLMIHSLYS NREIFLRELV SNASDACDKL RFEALDNGAL
YENDAELKIR IGFDAEAKTI TVADNGIGMS RDEAVAHLGT IAKSGTKEFF GQLTGDQKKD
AHLIGQFGVG FYSAFIVADK VTVVTRRAGL AAAEGVKWEC SMAGDEAGAY TVEQVEKAGR
GTQIILHLRE GQEDLLSSWK LKSLIRKYSD HIVQPIVMNK EEWNEEQQAQ VPTDEDETVN
QANALWTRAK NDITDDEYTA FYKHVGHDFE EPLAWTHSRV EGRHEYTNLL YIPKNAPFDL
WDRNARHGIK LYVKRVFIMD DAEKLMPTYL RFVRGVVDSA DLPLNVSREI LQESKDIDTI
RSGCTKKVLT LLESFANSDE AADQEKYATF WKAFGKVLKE GVGEDFANKD KIAGLLRFAS
TKADTPDEVV SLADYIGRMK EGQDKIYYVT AETFNAAKNS PHLEVFRKKD IEVLLLTDRV
DEWVTGNLTE FDGKALVSVA KGGLDLGALE DEAEKQEAEK AADEYKELLD KMKASLGERV
KDVKVTLRLT DSPACLVADE HDLGMNLARI LKAAGQNAPV SKPILEINPN HPAVLRLKYE
DRNFDDWAAV LFDQALLAEG GTLDDPATFV KRINQLMMAM SGN
//
