ID   A0A1G9E492_9ACTN        Unreviewed;       613 AA.
AC   A0A1G9E492;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SDK70945.1};
GN   ORFNames=SAMN05216298_1287 {ECO:0000313|EMBL:SDK70945.1};
OS   Glycomyces sambucus.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=380244 {ECO:0000313|EMBL:SDK70945.1, ECO:0000313|Proteomes:UP000198662};
RN   [1] {ECO:0000313|EMBL:SDK70945.1, ECO:0000313|Proteomes:UP000198662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3147 {ECO:0000313|EMBL:SDK70945.1,
RC   ECO:0000313|Proteomes:UP000198662};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; FNGF01000001; SDK70945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9E492; -.
DR   STRING; 380244.SAMN05216298_1287; -.
DR   Proteomes; UP000198662; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF26; HEAT SHOCK PROTEIN (HSP90 FAMILY)-RELATED; 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   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   613 AA;  67232 MW;  F04CE1059951D937 CRC64;
     MSETTPTSHT FQVDLRGLVD LLSHHLYSSP KVYVRELLQN AVDAITARRQ LDPEFDAAFD
     TDSAAVRITT DGRRLRITDP GVGLTIAEVH KLLATIGGSS KRDEEIEGAR RDFLGQFGIG
     LLACFTVASV ITVTSRSARD AAAPAVRWAA KDDGSYTVTE VPHAEHPEPG TTVELVARPG
     EDWLEPDRVV RLAREYGSLL PVAITVEPEG GAPVRITDTP PLWEREYPNP TARRLALNRY
     CEEVLGFAPL DVIDLDVPLS GLTGVAFVLP HATSPSARPA HRVHLKRMLL TDTADNLVPE
     WAFFVRCVVD TDSLRPTASR ESLYDDEALA VARDAVGAQI REWISRLAAE DPARLEAFLA
     VHELGVKALA RHDEELLAAM LPWLRFETTA GRTSLPEFAR AYQPVYLAGT VDEYRQVAQI
     AAAQGIGVVN GGYTYDAELV QALPRLDPQV KVEQLQPGVI SASLDPLDTR AELALQSFLA
     AARARLDAVD VDVVVREFNP VSVPALLLDD REARRERQRA EAEAQADDLW GGILASIKQH
     APRAQLVLNH RNPTVRRIGA IADPELAGTA VESLYGQALL MSHRPLRSAD TALLNRSFMN
     LLERVTKDER PQD
//