ID A0A318XM01_9FIRM Unreviewed; 661 AA.
AC A0A318XM01;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=LY28_01112 {ECO:0000313|EMBL:PYG88757.1};
OS Ruminiclostridium sufflavum DSM 19573.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=1121337 {ECO:0000313|EMBL:PYG88757.1, ECO:0000313|Proteomes:UP000248132};
RN [1] {ECO:0000313|EMBL:PYG88757.1, ECO:0000313|Proteomes:UP000248132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19573 {ECO:0000313|EMBL:PYG88757.1,
RC ECO:0000313|Proteomes:UP000248132};
RA Kyrpides N.;
RT "Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial
RT genomes (KMG-I) project.";
RL Submitted (JUN-2018) 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 GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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:PYG88757.1}.
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DR EMBL; QKMR01000005; PYG88757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318XM01; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000248132; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd01030; TOPRIM_TopoIIA_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
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 SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248132};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 434..557
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 661 AA; 75809 MW; 69557D95BF0D4C7E CRC64;
MTKGTGKTEY GNESISSLKG ADRVRLRPGV IFGSDGLDGC QHSFFEILSN SIDEAREGHG
NVIEVTRFAD HSIMVQDWGR GIPLDYNANE ERYNWELVYC ELYAGGKYKN NSGENYEYSL
GLNGLGACAT QYSSEYFDVT VFRDGYKYEL HFEKGQNAGE LKKEKCKYAQ TSTIQKWKPD
LEVFTDINIP LEYFQTVLKK QAVVNAGLRF VFKDEESGES FIYSYENGIV DYIKELSQED
GFTEVQFYEN ATKGRDREDK PEYKVKMQIA FCFNNKTNLL EYYHNSSFLE YGGAPDKAVK
NAMIYAIDKC IKERGRYNKD EAKLIFADIE DSLILVVNSF STVTSYENQT KKSITNKFIQ
EAMTTFLKEQ LEIYFIENKV ESDKIIEQVL VNKRSRETAE KTRINIKKKL SGNIDISNRV
KKFVDCRTKD ISRREIYIVE GDSALGSCKL GRDAEFQAIM PVRGKILNCL KADYDGIFKS
EIITDLLKVL GCGVEIKSKH NKDLNTFDMD SLRWNKIIIC TDADVDGFQI RTLILTMIYR
IVPTLLREGK VFIAESPLFE ITCKGKSYFA YSEKEKADIL ARLEGNKYAI QRSKGLGENE
PDMMWLTTMN PETRRLIKVM PSDVEEATRH MFDVLLGDNL PGRKQFIEEN GNKYLDMIDV
S
//
