ID A0A3L8Q012_9GAMM Unreviewed; 637 AA.
AC A0A3L8Q012;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ECO:0000313|EMBL:RLV61046.1};
GN ORFNames=D5018_04185 {ECO:0000313|EMBL:RLV61046.1};
OS Parashewanella curva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Parashewanella.
OX NCBI_TaxID=2338552 {ECO:0000313|EMBL:RLV61046.1, ECO:0000313|Proteomes:UP000281474};
RN [1] {ECO:0000313|EMBL:RLV61046.1, ECO:0000313|Proteomes:UP000281474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C51 {ECO:0000313|EMBL:RLV61046.1,
RC ECO:0000313|Proteomes:UP000281474};
RA Wang G.;
RT "Phylogeny of the Shewanellaceae, and recommendation for two new genera,
RT Pseudoshewanella and Parashewanella.";
RL Submitted (SEP-2018) 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:RLV61046.1}.
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DR EMBL; QZEI01000009; RLV61046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8Q012; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000281474; 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:UP000281474};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 27..184
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..345
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 563..637
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 637 AA; 71824 MW; 8B355BFCEDE947A1 CRC64;
MAQQETHGFQ TEVKQLLQLM IHSLYSNKEI FLRELVSNAA DAADKLRYNA LTNDALYEGD
GELRVRVSAN KEAGTVTIED NGIGMTRDGV IEHLGTIAKS GTAEFFSNLS GDAAKDSQLI
GQFGVGFYSA FIVAKKVAVE TRAAGHAAEE GVKWESEGEG EFSVEDITKK GRGTKITLFL
RDEEKEFADD WRLKSIITKY SDHISIPVEM WEEGKPESEG PDGEKIEATE GEWKGMNKAT
ALWTRNKSDI SDDEYNEFYK HVSHDYTDPL LWAHNRVEGK HEYTSLLYIP SKAPWDLWNR
DAKQGLKLFV QRVFIMDDAE SFMPSYLRFV KGLIDSNDLP LNVSREILQD NKVTQSMRSG
ITKRVLSMLE KLAKNDAEKY QKFYAEFGQV LKEGPAEDFA NKERIAGLLR FSSTNEDSSA
PTTSLEQYIE RMKEGQEKIY YIVADSYEAA AHSPHLELLR KKGIEVILMH DRIDEWLVNH
LNEFKEKKLH SVTQGDLELG DLEDKEEKEA AEKLAADSEA LVKRVKNVLA DKVSDVKVTT
RLTDTPACVV TGEGEMSSQM IKLMEAAGQA VPEVKPLFEI NPQHPLMERL DQEQDEEAFA
DWANLLLQQA QLSEKGSLAD PSNFIKLMNQ MLVASLK
//
