ID A0A1I4XTJ7_9PROT Unreviewed; 662 AA.
AC A0A1I4XTJ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN05216386_0282 {ECO:0000313|EMBL:SFN28723.1};
OS Nitrosospira briensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=35799 {ECO:0000313|EMBL:SFN28723.1, ECO:0000313|Proteomes:UP000183107};
RN [1] {ECO:0000313|Proteomes:UP000183107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nsp8 {ECO:0000313|Proteomes:UP000183107};
RA Varghese N.;
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; FOVJ01000001; SFN28723.1; -; Genomic_DNA.
DR RefSeq; WP_074793830.1; NZ_FOVJ01000001.1.
DR AlphaFoldDB; A0A1I4XTJ7; -.
DR STRING; 1266925.GCA_000619905_00598; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000183107; 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}; Reference proteome {ECO:0000313|Proteomes:UP000183107};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 30..187
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..343
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 373..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..662
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 517..546
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 662 AA; 75551 MW; B70CF4719DA72F4E CRC64;
MEATATKEHL SFQTEVKQLL KLMIHSLYSN KEIFLRELIS NASDAADKLR FEGLTDGALY
ESDSELKIRV SYDAAERTIT VADNGIGMSR QEVIDHIGTI AKSGTREFFS SLTGDQAKDA
HLIGQFGVGF YSAFIVSDKV TLITRRAGLR PEHGVRWESG GEGDYTLETV EKTDRGTQVI
LHLREGEDDL LNGWRLRSII RKYSDHITLP ILMKKEEWSQ EKNENTITDE DETVNQASAL
WARPKSEITP EQYNEFYKHV AHDFEPPLAY VHARVEGKQE YTQLLYIPSR APFDLYDRES
RHGIKLYVRR IFIMDDAKQL LPNYLRFVRG VIDSNDLPLN VSREILQESK DIEAIRAGAV
KKVLGLLEDL AQGQHEEQQD QQDQQDQQDR EGQEDEDKKG EGTKFETFWK EFGQVIKEGI
GEDYANRERI AKLLRFVSTH ADTDEQTVSL SDYLARMKEG QEKIYYVTAD SLKAARNSPH
LEVFRKKGIE VLLLSERVDE WLVANLTEFE GKQLQSVAKG SLDLGKLEDE AEKKEQEKEA
DEYKELTEKI KGILGEQVKD VRVTLRLTES PACLVADSHD MSGNLERLLK SAGQKVGHTK
PILEINPYHP MIQRLKSEEA HFTDWSHILF DQALLAEGGQ LDDPASFVKR INELFLSTAD
EE
//
