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Database: UniProt
Entry: R5WTE5_9BACT
LinkDB: R5WTE5_9BACT
Original site: R5WTE5_9BACT 
ID   R5WTE5_9BACT            Unreviewed;       686 AA.
AC   R5WTE5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein {ECO:0000313|EMBL:CCZ99191.1};
GN   ORFNames=BN505_00463 {ECO:0000313|EMBL:CCZ99191.1};
OS   Alistipes sp. CAG:157.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1262692 {ECO:0000313|EMBL:CCZ99191.1, ECO:0000313|Proteomes:UP000018346};
RN   [1] {ECO:0000313|EMBL:CCZ99191.1, ECO:0000313|Proteomes:UP000018346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:157 {ECO:0000313|Proteomes:UP000018346};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ99191.1}.
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DR   EMBL; CBAZ010000134; CCZ99191.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5WTE5; -.
DR   Proteomes; UP000018346; 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   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CCZ99191.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018346};
KW   Transferase {ECO:0000313|EMBL:CCZ99191.1}.
FT   COILED          582..639
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   686 AA;  78103 MW;  774C7CD4D2842A2A CRC64;
     MQNGKIGVTT ENIFPIIKKF LYSDHEIFLR ELVSNAVDAT QKLKTLASTG DYAGELGDLT
     VHVTADAAAR TLTISDAGIG MTAEEVDRYI NQIAFSGAEE FMSKYKNQNI IGHFGLGFYS
     AFMVADKVEI VTQSYREEAP TVVWSCGGTP EFTMTERAEK RSRGTDIILY LSEESAEFAD
     QSRIRGMLRK YCRFLPIPIA CGKVQEWKDG KYVDTERDDI VNDTDPLWTH NPADVTDEQY
     REFYRKLYPG SDDPLFWIHL NIDYPFHLTG ILYFPKIHNN FEIQKNRIQL YSNQVYVTDS
     VEGIVPEFLT LLHGVIDSPD IPLNVSRSYL QSDGNVRKIS GYITRKVADK LQELFNTARA
     DFEGKWDDLK IFIEYGIVTD EKFAEKAEGF MLLKNTAGSY FTLAEYRDKV KENQTDRNGT
     VIYIYTDDAV GKHSFVRGAE EKGYDVLLMD GQLDNHFVSW YENKEKGCRF VRVDSDVAER
     LIDKETNMSM SLSSEQQDIM RPVFESQLPT DQKIFYNIAF EAMAPTDAPV TITQDEYMRR
     MKEMAAMSGG GMSQFYSQMP DNYTIAVNAN HPLVIDILGV VENEYGEKLK TINKKIETAQ
     KQQANLNELI KDKKEADLTE EEKQQRDDLA KKVDDLRGQR TARLKEIGAG NSLVKQLIDL
     ALLSNGMLKG EQLTNFIKRS VELIGK
//
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