ID   A0A3D8Y5D3_9BACT        Unreviewed;       608 AA.
AC   A0A3D8Y5D3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:REA57672.1};
GN   ORFNames=DSL64_23330 {ECO:0000313|EMBL:REA57672.1};
OS   Dyadobacter luteus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=2259619 {ECO:0000313|EMBL:REA57672.1, ECO:0000313|Proteomes:UP000256373};
RN   [1] {ECO:0000313|EMBL:REA57672.1, ECO:0000313|Proteomes:UP000256373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS19 {ECO:0000313|EMBL:REA57672.1,
RC   ECO:0000313|Proteomes:UP000256373};
RA   Chen L.;
RT   "Dyadobacter roseus sp. nov., isolated from rose rhizosphere soil.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:REA57672.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QNUL01000026; REA57672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8Y5D3; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000256373; 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   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   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   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};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256373}.
SQ   SEQUENCE   608 AA;  69449 MW;  964CD6498D969041 CRC64;
     METGIQEKGN LSIHTENIFP IIKKFLYSDH EIFLRELVSN AVDATQKLKK LSSYGEFNGE
     LGELKVVVKL DKDAKTITIS DNGIGMTADE IKKYINQIAF SGATEFVEKY KDKGDEGKII
     GNFGLGFYSA YMVAKNVEII TKSYKDDSEA VRWECDGSTE FTLSSAEKAD RGSDIILHIA
     EDSEEFLDDY RLRGILEKYG KFLPIQIEFE DKVINNTSPI WTKNPSELKD EDYIAFYKEL
     YPMSEDPLFW IHLNVDYPFN LTGVLYFPKL KNDFQGQREK IQLYSRQVFI TDEVKDIVPD
     FLQLLHGVID SPDIPLNVSR SYLQADGNVK KINGYITRKV GDKLAEIFKN DRESFEAKFD
     DIGLFVKYGI VSDEKFYEKA KDFCLVKNVD GKFFTFSEYS ELVKENQTDK NDTQIWLYTT
     DEQKQDAFIQ SAKKRSYDVL SLTSVIDAHF INALEQKLEK TSVKRVDADT LDKLIEKDVK
     LESILSADDQ EKAKKLFEEV ADSKSAHIAV EAMPVDELPV VITFPEFMRR MTDMQATSGQ
     RSMFGDMPLM YTVSLNANHP IIGKVLQTEN EEEQKSLAKQ VYDLALLSQG LLTGSDLTKF
     IQRTVTTL
//