ID   D5EUV4_PRER2            Unreviewed;       890 AA.
AC   D5EUV4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Topoisomerase gyrA/parC subunit family protein {ECO:0000313|EMBL:ADE82989.1};
GN   OrderedLocusNames=PRU_0008 {ECO:0000313|EMBL:ADE82989.1};
OS   Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Xylanibacter.
OX   NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE82989.1, ECO:0000313|Proteomes:UP000000927};
RN   [1] {ECO:0000313|EMBL:ADE82989.1, ECO:0000313|Proteomes:UP000000927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX   PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG   North American Consortium for Rumen Bacteria;
RA   Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA   Coutinho P.M., Henrissat B., Nelson K.E.;
RT   "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT   bryantii: insights into their environmental niche.";
RL   Microb. Ecol. 60:721-729(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002006; ADE82989.1; -; Genomic_DNA.
DR   RefSeq; WP_013064975.1; NC_014033.1.
DR   AlphaFoldDB; D5EUV4; -.
DR   STRING; 264731.PRU_0008; -.
DR   KEGG; pru:PRU_0008; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_015760_0_0_10; -.
DR   Proteomes; UP000000927; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000927};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          29..465
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          838..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          433..464
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        851..865
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   890 AA;  101623 MW;  4005EE062ABD4607 CRC64;
     MDDEIKEIEQ SEQHSDYKPS NRFDAAAVHH LSGMYQNWFL DYASYVILER AVPHLGDGLK
     PVQRRILHSM KRMDDGRYNK VANIVGHTMQ FHPHGDASIG DALVQLGQKD LLIDTQGNWG
     NILTGSSAAA PRYIEARLSK FALDTVFNPK TTEWKMSYDG RNKEPITLPV KFPLLLAQGA
     EGIAVGLSSK ILPHNFCEIC DAAISYLHQQ PFALYPDFPT SGSIDVSKYN DGQRGGVIKV
     RAKIEKIDQK TLVIREIPFS KTSETLQDSI VKAIEKGKIK ARKVEDLTAA EVEIQVHLAP
     GVSSDKTIDA LYAFTDCEVS ISPNCCVIED NKPQFLTVSD VLRHSVERTK DLIRQELEIR
     KGELLEQLHF QSLERIFIEE RIYKDKKFEQ APNVDAVCEH IDERLTPYYP QFIREVTKDD
     ILKLLEIKMQ RILKFNKDKA DELMARLKAE IEEIDRDLAN LVEVTANWFQ FLKDKYGKDH
     PRLTEIRNFD TIDSAKVAEA NQKLYINRSD GFIGTGLKKD EFVCNCSDLD DVIIFYKDGK
     YKIVRVAEKL FVGKNILYVN VFKKNDSRTI YNAVYRDGKK GACYIKRFNV TSMTRDKEYD
     LTQGTDGSRV MYFTANPNGE AEVIKVTLDP SQNIKRVFLV KDFSEIMIKG RASKGNLLTK
     YQVTRIGLKS HGHSTLGGRK VWFDPDVNRL NYDDHGKMLG EFYDDDQILV ILSNGDYYLS
     NFDLANHYES NILRIEKYDA DKVWTAVLYD ADNQGYPYLK RFQMDATKKK QNWLSDNPAS
     QLLLLTDTPY PRLQVTYGGA DAFRGSEEID AEQFIAVKGY KAKGKRLTTY ALENIEELEP
     TRFPEPPAET ADADTEPEEE DLDPDAGKSE QQIRDELTGQ LNLFDNEDFK
//