ID F2WZ87_FLAPS Unreviewed; 437 AA.
AC F2WZ87;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:ADZ57486.1};
OS Flavobacterium psychrophilum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=96345 {ECO:0000313|EMBL:ADZ57486.1};
RN [1] {ECO:0000313|EMBL:ADZ57486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F.nr 4695 {ECO:0000313|EMBL:ADZ57486.1};
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:ADZ57486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F.nr 4695 {ECO:0000313|EMBL:ADZ57486.1};
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; HQ283342; ADZ57486.1; -; Genomic_DNA.
DR AlphaFoldDB; F2WZ87; -.
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 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:ADZ57486.1}.
FT DOMAIN 227..337
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADZ57486.1"
FT NON_TER 437
FT /evidence="ECO:0000313|EMBL:ADZ57486.1"
SQ SEQUENCE 437 AA; 50262 MW; 928B89D30BA5ACCD CRC64;
YIIKMLKNYC YLNTGLTIIY NGEKFFSNNG LKDLLEENIA EEDMVYPIIH LLGDDIEIAI
THSKTQYSEE YYSFVNGQNT TQGGTHLGAF RESIVKTIKE FYNKPFEASD IRKSIVSAIV
VRVEEPVFES QTKTKLGSTD MGPDLPSVRT FVNDFIKTKL DNFLHKNPET ADLLLRKILQ
AERERKELSG IRKLAKDRAK KSNLHNKKLR DCRVHLTDAK NARSLESTLF ITEGDSASGS
ITKSRDVNTQ AVFSLRGKPL NSYGMSKKIV YENEEFNLLQ AALNIEESME DLRYNNIVIA
TDADVDGMHI RLLLITFFLQ FFPEMIKEGH LYILQTPLFR VRNKKETIYC YSEQEKRDAI
EKLKPKPEIT RFKGLGEISP DEFKNFIGET IRLDPVMLDK STSIEKLLEF YMGKNTPDRQ
TFIINNLKVE LDVVEAN
//