ID A0A1C6SI06_9ACTN Unreviewed; 633 AA.
AC A0A1C6SI06;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=GA0070624_3821 {ECO:0000313|EMBL:SCL29111.1};
OS Micromonospora rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=568872 {ECO:0000313|EMBL:SCL29111.1, ECO:0000313|Proteomes:UP000199413};
RN [1] {ECO:0000313|Proteomes:UP000199413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45431 {ECO:0000313|Proteomes:UP000199413};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-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; FMHV01000002; SCL29111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6SI06; -.
DR STRING; 568872.GA0070624_3821; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000199413; 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:UP000199413};
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..343
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 556..633
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 633 AA; 71192 MW; 4979627235843D76 CRC64;
MSDRVETLEF QAEARQLLQL MVHSIYSNKD IFLRELISNA SDALDKLRLE SMIDKELAAD
VSDLHIELEV DKDARTLTVR DNGIGMSRDE VVRLIGTIAK SGTAELLGKL RESSDAGASQ
ELIGQFGVGF YATFMVADEV TLLTRRAGES GGTRWESTGE GTYTIEAVDD APQGTSVTLH
LKPADAEDNL HDYTTEWTIR QIVKRYSDFI AWPIRMTVER SGEDGATTSE VQTLNSMKAL
WARSRDEVDE AEYKEFYKHV SHDWADPLET IHMRGEGTFE YEALLFLPSH APLDMFAPQG
RRGVQLYVKR VFIMDDCDAL MPNYLRFVKG VVDAHDLSLN ISREILQQDR QIRAVRRRLV
KKVLATLKVM KTAQAERYRT FWTEFGAVVK EGLLEDADNT EAILDLVQVA STHDPAEPTT
LRDYVERMKD GQGDIYYATG ESRSMIENSP HMEAFRAKGY EVLILTDPVD EVWVERVGQF
DGKPLRSIAK GEVDLETDEE KEKAEAERKD FAELLSWMSG KLADSVKEVR LSSRLTTSPA
CVVGDAHDMT PTLEKMYRAM GQEVPRVKRI LELNPSHPLV TGLRKAHEQG AESESLAETA
ELLYGMALLA EGGELADPSR FTRILADRLA RTL
//
