ID F2WZ79_FLAPS Unreviewed; 456 AA.
AC F2WZ79;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN Name=parE {ECO:0000313|EMBL:ADZ57478.1};
OS Flavobacterium psychrophilum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=96345 {ECO:0000313|EMBL:ADZ57478.1};
RN [1] {ECO:0000313|EMBL:ADZ57478.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F.nr 5005 {ECO:0000313|EMBL:ADZ57478.1};
RA Shah S.Q.A., Nilsen H., Bottolfsen K., Colquhoun D.J., Sorum H.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADZ57478.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F.nr 5005 {ECO:0000313|EMBL:ADZ57478.1};
RX PubMed=22283604; DOI=10.1089/mdr.2011.0142;
RA Shah S.Q., Nilsen H., Bottolfsen K., Colquhoun D.J., Sorum H.;
RT "DNA Gyrase and Topoisomerase IV Mutations in Quinolone-Resistant
RT Flavobacterium psychrophilum Isolated from Diseased Salmonids in Norway.";
RL Microb. Drug Resist. 18:207-214(2012).
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};
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DR EMBL; HQ283334; ADZ57478.1; -; Genomic_DNA.
DR AlphaFoldDB; F2WZ79; -.
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; cd00822; TopoII_Trans_DNA_gyrase; 1.
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; 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; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 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 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADZ57478.1}.
FT DOMAIN 246..356
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADZ57478.1"
FT NON_TER 456
FT /evidence="ECO:0000313|EMBL:ADZ57478.1"
SQ SEQUENCE 456 AA; 52566 MW; 490B80E6C082E72F CRC64;
KVSFIADEAI FKNYKYRNEY IIKMLKNYCY LNTGLTIIYN GEKFFSNNGL KDLLEENIAE
EDMVYPIIHL LGDDIEIAIT HSKTQYSEEY YSFVNGQNTT QGGTHLGAFR ESIVKTIKEF
YNKPFEASDI RKSIVSAIVV RVEEPVFESQ TKTKLGSTDM GPDLPSVRTF VNDFIKTKLD
NFLHKNPETA DLLLRKILQA ERERKELSGI RKLAKDRAKK SNLHNKKLRD CRVHLTDAKN
ARSLESTLFI TEGDSASGSI TKSRDVNTQA VFSLRGKPLN SYGMSKKIVY ENEEFNLLQA
ALNIEESMED LRYNTIVIAT DADVDGMHIR LLLITFFLQF FPEMIKEGHL YILQTPLFRV
RNKKETIYCY SEQEKRDAIE KLKPKPEITR FKGLGEISPD EFKNFIGETI RLDPVMLDKS
TSIEKLLEFY MGKNTPDRQT FIINNLKVEL DVVEAN
//
