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Database: UniProt
Entry: E1KSN8_9BACT
LinkDB: E1KSN8_9BACT
Original site: E1KSN8_9BACT 
ID   E1KSN8_9BACT            Unreviewed;       684 AA.
AC   E1KSN8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein {ECO:0000313|EMBL:EFL45579.1};
GN   ORFNames=HMPREF9296_1699 {ECO:0000313|EMBL:EFL45579.1};
OS   Prevotella disiens FB035-09AN.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=866771 {ECO:0000313|EMBL:EFL45579.1, ECO:0000313|Proteomes:UP000003610};
RN   [1] {ECO:0000313|EMBL:EFL45579.1, ECO:0000313|Proteomes:UP000003610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB035-09AN {ECO:0000313|EMBL:EFL45579.1,
RC   ECO:0000313|Proteomes:UP000003610};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) 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:EFL45579.1}.
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DR   EMBL; AEDO01000046; EFL45579.1; -; Genomic_DNA.
DR   RefSeq; WP_004357283.1; NZ_AEDO01000046.1.
DR   AlphaFoldDB; E1KSN8; -.
DR   STRING; 866771.HMPREF9296_1699; -.
DR   eggNOG; COG0326; Bacteria.
DR   Proteomes; UP000003610; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 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; 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   Kinase {ECO:0000313|EMBL:EFL45579.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000313|EMBL:EFL45579.1}.
FT   REGION          608..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  78451 MW;  2C139EB538990D50 CRC64;
     MQKGKIGVTT ENIFPVIKKF LYSDHEIFLR EMVSNAVDAT QKLRTLATTG EFKGETNDLK
     VNVKLDEKAG TLTISDNGIG MTAEEIEKYI NQIAFSGVTD FLDKYKDKAE AIIGHFGLGF
     YSSFMVAKKV EIITKSYREG AQAVKWSCDG SPEFSLEEVE KEGRGSDIVL YIDDDCKEFL
     EKQKIEGLLN KYCKFMSVPV VFGKRSEWKD GKMEDTDEDN IINNVEPLWA KTPSGLKDED
     YKSFYRTLFP MNDEPLFWIH LNVDYPFNLT GILYFPRVKN NIELQRNKIQ LFCNQVFVTD
     QVEGIVPEFL TLLHGVIDSP DIPLNVSRSY LQSDANVKKI SSYITKKVAD RLNSIFKENR
     KEYEEKWADL KLFVNYGMLS QPDFYDRAKD FSFLTDVDGK NFTYEEYKTL IKDNQTDKEG
     NLIYLYANDK EEQFSYIEAA KAKGYSVILA DGQLDVPAVS MLEQKFEKSR FVRVDSDVID
     RIIAKDDKPE QKLSDNERDI LSEAFQSQMP QMEKAQFMVE IEAMGETAQP VIVTQNEYMR
     RMKEMSQYQQ GMGFYAQMPD NYTLVLNSDH ALVKRILEEG SANTAEALKP ILSEIKGLQA
     RETILRQEQG KKKAEEITQE EKDDLKGTED KLGEQRKQKN EIIAEYAKGN DSIHQLIDLA
     LLQNGMLKGA ALDKFIKRSV DLIK
//
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