ID A0A1G6I356_9PSEU Unreviewed; 632 AA.
AC A0A1G6I356;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=DES30_1011294 {ECO:0000313|EMBL:PWV85267.1},
GN SAMN05421630_10144 {ECO:0000313|EMBL:SDC00979.1};
OS Prauserella marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=530584 {ECO:0000313|EMBL:SDC00979.1, ECO:0000313|Proteomes:UP000199494};
RN [1] {ECO:0000313|EMBL:SDC00979.1, ECO:0000313|Proteomes:UP000199494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5506 {ECO:0000313|EMBL:SDC00979.1,
RC ECO:0000313|Proteomes:UP000199494};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWV85267.1, ECO:0000313|Proteomes:UP000246674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45268 {ECO:0000313|EMBL:PWV85267.1,
RC ECO:0000313|Proteomes:UP000246674};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-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}.
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DR EMBL; QGTN01000001; PWV85267.1; -; Genomic_DNA.
DR EMBL; FMZE01000001; SDC00979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6I356; -.
DR STRING; 530584.SAMN05421630_10144; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000199494; Unassembled WGS sequence.
DR Proteomes; UP000246674; 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:UP000199494};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 28..185
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..337
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 338..553
FT /note="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 485..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..632
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 632 AA; 71360 MW; 4A9520D524707EB1 CRC64;
MATQTETLEF QAEARQLLQL MVHSIYSNKD IFLRELISNA SDALDKLRLS AFKDKDLDVD
VSDLRIDIET DPERRTLTVR DNGIGMSRDE VVGLIGTIAK SGTAELLRTL RESKDSEASR
ELIGQFGVGF YSSFMVADRV TLLTRRAGES DGTRWESRGE GTYTIDTVPG APQGTAVTLH
LKPEDAEDQL HDYTSRAKIK EIVRRYSDFI TWPIRMETGE EGEEAEILNS RKALWARPKD
ETTEEEYREL YKHLSHDWAD PLETIQFMAE GTFEYQALLF IPSRAPLDLF MRDAKRGVQL
YVKRVFIMDD CEELMPEYLR FVKGVVDAQD LSLNVSREIL QQDRHIRLMR RRLVKKVLGS
VKGMLTDKPE QYDTFWREFG KAVKEGIVTD ADNQEAILDI ASFETTHDPE RPTTLARYVE
RMKEGQEHIY YLTGASRSVI EKSPHMEALR AKGFEVLLLT DPIDEMWAGS VTGFAGKTFQ
SIAKGQVDLP GGDDETESES ERTEQRRNFA PLLEWMTTTL EEHIKEVRLS TRLTSSPACI
VGETYDISPA LAKMYEAAGQ EVPSAKRILE LNPDHPLVAG LRAAHAGETK DTAALAETVE
LLYGMALLAE GSELLDPQRF TALLADKLTG TL
//
