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Database: UniProt
Entry: F2WZ87_FLAPS
LinkDB: F2WZ87_FLAPS
Original site: F2WZ87_FLAPS 
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
//
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