ID A0A1C6RZZ3_9ACTN Unreviewed; 637 AA.
AC A0A1C6RZZ3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=GA0074692_1425 {ECO:0000313|EMBL:SCL22610.1};
OS Micromonospora pallida.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=145854 {ECO:0000313|EMBL:SCL22610.1, ECO:0000313|Proteomes:UP000198959};
RN [1] {ECO:0000313|EMBL:SCL22610.1, ECO:0000313|Proteomes:UP000198959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43817 {ECO:0000313|EMBL:SCL22610.1,
RC ECO:0000313|Proteomes:UP000198959};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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}.
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DR EMBL; FMHW01000002; SCL22610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6RZZ3; -.
DR STRING; 145854.GA0074692_1425; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000198959; 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}; 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 344..559
FT /note="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 560..637
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 637 AA; 72566 MW; DB98FEDB573BAEE8 CRC64;
MSNGVETREF QAEARQLLQL MVHSIYSNKD VFLRELVSNA SDALDKLRLE SMVDKELDVD
TSDLHVAIEV DKEQRTLTVR DNGIGMSRDD VVTLIGTIAK SGTAELLRKL RESQDASASQ
DLIGQFGVGF YATFMVADRV ELVSRRAGEA GGTRWESTGE GTYTIEAVDD VPQGTSVTVH
LKPEDSEDNL FDYTADWKIR EIVKRYSDFI AWPIRMAVER TDAEGEATTE VQTLNSMKAL
WARPRSEVDE AEYQEFYKHV SHDWADPLEI IHMRGEGTFE YEALLFLPSH APFDLFAREG
RRGVQLYVKR VFIMDDCEAL MPDYLRFVKG VVDAHDLSLN ISREILQQDR QIRAVRRRLV
KKVLSTVRTM MTEHPDRYRT FWTEFGRAVK EGLIDDTENR DTLLEITSLA STRDETELTT
LAQYVERMKD GQADIYYMTG ESRAMIENSP HMEAFRAKGY EVLVLTDPVD EVWIERVGEF
DGRPLRSIAK GQVDLDTEEE KKTAEPEREQ QRKDFESLLT WLGEQLSEQV KEVRLSSRLT
TSPACIVGDA YDMTPTLEKM YRAMGQDVPS VKRILELNPT HPLVTGLRTA YEQDGDKEVL
TETAELLHGM ALLAEGGELS DPARFTRILA DRLARTL
//
