ID A0A074KW30_9BACT Unreviewed; 627 AA.
AC A0A074KW30;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Molecular chaperone Hsp90 {ECO:0000313|EMBL:KEO73114.1};
GN ORFNames=EL17_16015 {ECO:0000313|EMBL:KEO73114.1};
OS Anditalea andensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO73114.1, ECO:0000313|Proteomes:UP000027821};
RN [1] {ECO:0000313|EMBL:KEO73114.1, ECO:0000313|Proteomes:UP000027821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY1 {ECO:0000313|EMBL:KEO73114.1,
RC ECO:0000313|Proteomes:UP000027821};
RA Yang L., Wei S., Tay Q.X.M.;
RT "Characterization and application of a salt tolerant electro-active
RT bacterium.";
RL Submitted (APR-2014) 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:KEO73114.1}.
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DR EMBL; JMIH01000023; KEO73114.1; -; Genomic_DNA.
DR RefSeq; WP_035076445.1; NZ_JMIH01000023.1.
DR AlphaFoldDB; A0A074KW30; -.
DR STRING; 1048983.EL17_16015; -.
DR eggNOG; COG0326; Bacteria.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000027821; 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; 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.
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:UP000027821}.
SQ SEQUENCE 627 AA; 71913 MW; 910F650D430879C7 CRC64;
MQEKGTISIH TENIFPIIKK FLYSDNEIFL RELVSNSVDA TQKMKRLATL GQYTGDLGDT
TVEVSFDKEK KTITISDRGL GMTAEEIKKY INQIAFSGAA EFVEKFKDAK DANEIIGKFG
LGFYSAFMVA HTVEINSLSY QEGAESAKWI CDGSTQFEIS EGTRTERGTE VILHINEESE
EFLDKWKLQG ILDKYCKFLP VPIKFGTKTD SVEDGKDEEG KTKYKSVESD NIINTTSPIW
TKSPNELTDE DYLSFYKELY PMSEDPLFWI HLNVDYPFNL TGVLYFPKVK NEFELQKNKI
KLFSRQVFIT DEVKDIVPEF LMLLHGVIDS PDIPLNVSRS FLQADSNVKK INNYITKKVA
DKLGELYKKD RKGYEEKWND IGLFVKYGMI SEDKFYEKGK DFALVKNTRG EFFTIEEYKE
KVKPTQTDKD EQTIFLYATD TDKQDSFIQS ANKKDYDVLV MDSPIDSHFI QQLEQKLEKT
SLKRVDADVA DKLINKEESF ANVLTEEQST KVKEVFEKAL DNKSFSVEVE GLNPDELPVT
ITMEEFMRRM KDMAQTGGGM GFYGQLPDHY KVAINGNHKV VDKILKAENE EDQTRLAKQA
VDLAMLSQGM LKGKDLTEFV RRSVEMI
//
