ID B5CQM2_9FIRM Unreviewed; 748 AA.
AC B5CQM2;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=RUMLAC_01769 {ECO:0000313|EMBL:EDY32449.1};
OS [Ruminococcus] lactaris ATCC 29176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=471875 {ECO:0000313|EMBL:EDY32449.1, ECO:0000313|Proteomes:UP000003254};
RN [1] {ECO:0000313|EMBL:EDY32449.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY32449.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus lactaris ATCC 29176.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDY32449.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY32449.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:EDY32449.1}.
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DR EMBL; ABOU02000039; EDY32449.1; -; Genomic_DNA.
DR AlphaFoldDB; B5CQM2; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR Proteomes; UP000003254; Unassembled WGS sequence.
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 CDD; cd00187; TOP4c; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
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; PF03989; DNA_gyraseA_C; 2.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 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, ECO:0000313|EMBL:EDY32449.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003254};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 12..487
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 459..500
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 748 AA; 84847 MW; 33909D86D0B0A296 CRC64;
MKMNSESQII RTEYSELMKK SYIDYAMSVI IARALPDVRD GLKPVQRRTL YDMYELGIRY
DKPYRKCARI VGDTMGKYHP HGDSSIYDAL AVMAQDFKKG QILVDGHGNF GSIEGDGAAA
MRYTEARLTK FTQEVCLSDL DKNVIDFGPN FDETEKEPVV LPMRVPNLLV NGAEGIAVGM
ATSIPTHNLC EVIDGVKAYM KNDGVTTRQL MKYIKGPDFP TGGIVVNKDD LLNIYETGQG
KIKLRGKVEV EDLKGGKKQL VITEIPYTMI GAGIGKFLND VCNLVETKKT TDIVDISNQS
SKEGIRIVIE LKRGADVENL KNMLYKKTRL EDTFGVNMLA VANGRPETLG LKQIIEHHVD
FQFELATRKY TTLLEREREK SEVQEGLIKA CDVIDLIIEI LRGSKSVKDA RACLVEGKTE
NIRFKFSISK KMAAMLRFTE RQATAILEMR LYRLIGLEIE ALQKEHEQTL NNIARYEDIL
NNYDSMAEVI MEELDSYKKE FGRKRRTVVE NAEEAVFEEK KVEEQEVVFL MDRFGYAKTV
DMAVYERNKE AADSENKYIV HCMNTGKLCI FTDTGKMHQV KVLDLPYGKF REKGTPIDNV
SNYTSSEEEI VMICDAEQMR FAKLLFATAQ GMIKRVDGKE FQVAKRTIVA TKLQEDDRLV
SVKVVNETQN LVLQTRNGYF LRFPAADVPE KKKAAVGVRG IRLQKKDELE HTYLFEEGTE
TKVTYGEKTV TLNRLKAAKR DGVGNKTR
//
