ID A0A1H5PU61_9ACTN Unreviewed; 648 AA.
AC A0A1H5PU61;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN05216533_8300 {ECO:0000313|EMBL:SEF17383.1};
OS Streptomyces sp. Ag109_O5-10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEF17383.1, ECO:0000313|Proteomes:UP000198812};
RN [1] {ECO:0000313|EMBL:SEF17383.1, ECO:0000313|Proteomes:UP000198812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEF17383.1,
RC ECO:0000313|Proteomes:UP000198812};
RA de Groot N.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; FNTQ01000001; SEF17383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5PU61; -.
DR STRING; 1855349.SAMN05216533_8300; -.
DR Proteomes; UP000198812; 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:UP000198812};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 37..195
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..353
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 571..648
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 648 AA; 72250 MW; AAA2880A4DF677F2 CRC64;
MTIPQKETHM GSSAETLEFQ AETRQLLRLV IHSIYSNKDI FLRELISNAS DALDKLRLES
LTDSGLTEID TADLHITLEV DKDARTLTVR DNGIGMTRDD LVDLIGTIAK SGTAGLLEKI
KESKDAATVE NLIGQFGVGF YSAFMVADKV TLRTRRAGTG SGTQWESDGE GTYDLQSVDG
LPVGTSVTLH LKPADSEDGL ADYLSESKIR QIVKRYSDFI RWPIRMATER SDAEGETTSG
IDTLNSMKAL WGRPRSEVTE GEYNEFYQQI SHDWLPPAET IHMRAEGTFE YEALLFIPSQ
APFDLFSRET KPGVQLYVKR VFIMDDCEAL MPNYLRFVKG VVDAHDLSLN VSREILQHDR
QIRGVRRRLV KKVLGAIKDM QSKDAERYAK VWAQFGRALK EGLLEDTDNT ETLLELLSAA
STHDPEKTTT LREYVERMKD GQDTIYYLTG ESRAMVENSP HMEAFAAKGY EVLILTDPVD
EVWVDQIPAF DGHRLQSIAK GQVDLDESAD GDQDSDAEKV QREQDFAALL PWLTTTLSEQ
VKQVRLSSRL TTSAACIVGD AHDVTPTLEK MYRAMGQQIP PVKRILELNP AHPLVNALRT
AHDAGADDPA LAEIAELIYG SALLAEGGDL PDPARFTRLL TDRLTHTL
//
