ID A8UQE8_9FLAO Unreviewed; 637 AA.
AC A8UQE8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 08-NOV-2023, entry version 77.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:EDP69478.1};
GN ORFNames=FBALC1_05283 {ECO:0000313|EMBL:EDP69478.1};
OS Flavobacteriales bacterium ALC-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP69478.1, ECO:0000313|Proteomes:UP000003630};
RN [1] {ECO:0000313|EMBL:EDP69478.1, ECO:0000313|Proteomes:UP000003630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALC-1 {ECO:0000313|EMBL:EDP69478.1,
RC ECO:0000313|Proteomes:UP000003630};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP69478.1}.
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DR EMBL; ABHI01000008; EDP69478.1; -; Genomic_DNA.
DR AlphaFoldDB; A8UQE8; -.
DR STRING; 391603.FBALC1_05283; -.
DR eggNOG; COG0326; Bacteria.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000003630; 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; 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:UP000003630};
KW Stress response {ECO:0000313|EMBL:EDP69478.1}.
FT REGION 207..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 72748 MW; A48ED55E08C29046 CRC64;
MTKGSINVSV ENIFPLIKKF LYSDHEIFLR ELISNGTDAT LKLKHLTSIG ESKSEYGNPQ
IEVKIDKDQK KLHIIDQGLG MTAEEVEKYI NQVAFSGAEE FLDKYKDSAQ DSGIIGHFGL
GFYSAFMVAE KVEILTKSHK DEPAAHWTCD GSPEFTLVEA DKEDRGTEIV LHIAEDSTEF
LEEARIRELL NKYNKFMPIP IKFGTKEVND PEFTPQTTTD AEGKETTEPH KQITVDDIIN
NPNPAWTKQP ADLKDEDYSG FYRELYPMQF EEPLFNIHLN VDYPFNLTGI LYFPKMTNDL
NIQKDKIQLY QNQVFVTDNV EGIVPEFLTM LRGVIDSPDI PLNVSRSYLQ ADGNVKKISS
YITRKVADKL KSLFNNSRED FEKKWDDIKI VIEYGMLSEE KFFEKADAFA LYPTVDGKYY
TFEELTNAIK AKQTDKDDKM VILYASNKDE QHSYIESAKA KGYEVLMLDS PIVSHLIQKL
ETTKENISFA RVDGDHIDNL IKKDETAISK LTDEEKTKLD EVLKAVVPSE KFMVQLEAMD
SDASPFIITQ PEFMRRMKEM QQTGGGGGMF GMGNMPEMYN LIVNTNSELV GEILNTKTKK
KQERLINQSL DLARLSQGLL KGEELTNFIK RSYDMIK
//