ID A0A1G8W187_9BURK Unreviewed; 681 AA.
AC A0A1G8W187;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05444748_11962 {ECO:0000313|EMBL:SDJ71813.1};
OS Variovorax sp. OV700.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882826 {ECO:0000313|EMBL:SDJ71813.1, ECO:0000313|Proteomes:UP000199505};
RN [1] {ECO:0000313|Proteomes:UP000199505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV700 {ECO:0000313|Proteomes:UP000199505};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNDR01000019; SDJ71813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8W187; -.
DR STRING; 1882826.SAMN05444748_11962; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000199505; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 29..186
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 377..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..681
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 681 AA; 75169 MW; 5F9E0F6FF5775B27 CRC64;
MADSSNTKLP FQAEVAQLLH LVTHALYSNK EIFLRELISN ASDACDKLRF EAIDHPALYE
DQPNLDVRLS FDKAARTITI TDKGIGLSRQ EAIDHLGTIA KSGTKDFMSK LSGDQKADAQ
LIGQFGVGFY SGFIVADKIT VESRRAGLSP EQGVRWVSGG AGDFEVADIT RAERGTSITL
HLRDDADEYL NAWKLKQIVG KYSDHISLPI LMEKEEWKEG ENDQPGDMVK TGEWETVNKA
NALWSRNKKD ITPEQYEEFY KTVSHDYEAP LAWSHNRVEG STEYTQLLYI PSKAPFDLWN
REKSAGVKLY VKRVFIMDDA EALLPSYLRF VKGVIDSSDL PLNVSRELLQ ESRDVKAIRE
GSTKRVLSML EDLAKKQKTA PESAEGKIDV GSGESVPAPD PTEIAADVTD VVDKKAMPAA
EAAAEYADES GKYAKFYAEF GAVLKEGLGE DFTNRDRIAK LLRFASTTSD TVSVSFADYK
ARMKEGQDAI YYITADTLAA AKNSPQLEVF KKKGIEVLLM TDRVDEWALN YLTEFDGTPL
QSVAKGAVDL GKLQDEAEKK AAEEAAESFK PLLEKLKEAL KDKAEDVRVT TRLVDSPACL
VVQDGGMSTQ LARMLKQAGQ PAPDLKPVLE VNAEHPLVKK LEGSAHFDDL ANILFDQALL
AEGGLPADPA AYVRRVNALL V
//
