ID A0A1V2ZW76_9GAMM Unreviewed; 637 AA.
AC A0A1V2ZW76;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=B1A74_11575 {ECO:0000313|EMBL:OOC09378.1};
OS Thioalkalivibrio halophilus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=252474 {ECO:0000313|EMBL:OOC09378.1, ECO:0000313|Proteomes:UP000189177};
RN [1] {ECO:0000313|EMBL:OOC09378.1, ECO:0000313|Proteomes:UP000189177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL17 {ECO:0000313|EMBL:OOC09378.1,
RC ECO:0000313|Proteomes:UP000189177};
RA Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA Sorokin D.Y., Muyzer G.;
RT "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio.";
RL Submitted (FEB-2017) 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:OOC09378.1}.
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DR EMBL; MUZR01000051; OOC09378.1; -; Genomic_DNA.
DR RefSeq; WP_077244730.1; NZ_MUZR01000051.1.
DR AlphaFoldDB; A0A1V2ZW76; -.
DR STRING; 252474.B1A74_11575; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000189177; 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}; Reference proteome {ECO:0000313|Proteomes:UP000189177};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 35..192
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 499..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..637
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COMPBIAS 500..515
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71976 MW; D63C10BAB1D04337 CRC64;
MTETRTEQAA EAETRQFETE VSQLLQLMIH SLYSNREIFL RELISNGADA CDKLRFEATA
NPDAIPQPAE LHIDVDVDKD ARTVTVHDNG IGMSRDEVIR QIGTIAHSGT RAFLEKLTGD
QQKDAQLIGQ FGVGFYSSFI VADHVRVETR RAGTGVEAGT RWESKGDGEY TLSDCERAEP
GTEITLTLKE DADEFLEPMR LRHVIGRYSD HVAFPIRMRK QDDEGNPTDE WETVNRASAL
WTRPKSEISD EEYREFYKHI AHDFEDPVAW THNHVEGRQE YTTLFYIPGR APFDLWDRDA
RHGVKLYVKR VFIMDDAEKL LPNYLRFVRG VVDSSDLPLN VSREILQDNR LVDSIRSGSV
KKILGLLENI AKNEPEKYAG IWDNFGRVLK EGPGEDFANQ QQIAGLLRFA STYNDDDTQN
VSFADYKARM KEGQDAIYVI SADNAAAARN SPHLEVFRKH GIEVLLLSDR VDEWLLSNLR
EFDGTPIKNV AKGDLDLDNI IGEQDSDDAD NTEDRKDDEL GDLPERIQSA LGDRVDSVRP
SKRLVDSPAC IVLGEHEMAL YLQELLKQAG QETFSSKPVL EVNAQHPLVE RLKTAEGDDF
NDLASLLFEQ SLLAEGGQLE DPSGFVHRLN RFLLQAG
//
