ID A0A150AKU1_9BACT Unreviewed; 624 AA.
AC A0A150AKU1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:KXX70208.1};
GN ORFNames=AVL50_15195 {ECO:0000313|EMBL:KXX70208.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX70208.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX70208.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX70208.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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:KXX70208.1}.
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DR EMBL; LQAQ01000061; KXX70208.1; -; Genomic_DNA.
DR RefSeq; WP_062617427.1; NZ_LQAQ01000061.1.
DR AlphaFoldDB; A0A150AKU1; -.
DR STRING; 1775430.AVL50_15195; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000075267; 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:UP000075267}.
SQ SEQUENCE 624 AA; 71101 MW; 779511E52980241C CRC64;
MAAKGSISVN TENIFPIIKK FLYSDHDIFL RELVANAVDA TQKLQKLASM GEFDGELGDL
TIQVDVDKEA KTISITDRGI GMSEDEVEKY INQVAFSGAT EFVEKFKDVD TSTIIGKFGL
GFYSAFMVSD HVEVITKSFK DAPSVKWTCD GSTTYEITDA DKADRGTTIV LHVNEDSEEF
VDEHRLRTIL NRYSKFMPIA IQVGVDKRTE KEGEGDDAKD VEIVEPHIIN QKEPLWTKDP
KTLTDEDYIN FYKELYPMSE EPLFWIHLNV DYPFELTGIL YFPKVKEDIT PHKDKIQLYS
RQVFITDNVE EIMPEFLRLM HGVIDSPDIP LNVSRSYLQS DANVKKISSY VTRKVADRLS
SLFKNERESY ETKWESIGLF VKYGMMTDDK FFDKAKKFGL FENIDGKKFT LEEYKEHIAS
NQIDKDGKHV FLYATDQGTQ DTYIQAAKKK GYDILKMDTM IDSHFVSNTE HKFENITMKR
IDSDTVNNLI ETDEKNESVL TEDETKKLVE IFKRALNDDK LEPKVEAMTA DELPVMITKP
EFMRRMEEMS AMQGGMGGMF GGFPGADTVT INGNSELVGR ILKEEDTAAQ DKLVKHAYDL
AKLSQGNLKG ADLTAFINRS LEII
//
