ID Q9AJI7_9BACT Unreviewed; 474 AA.
AC Q9AJI7;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 102.
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=gyrB {ECO:0000313|EMBL:BAB40402.1};
OS marine CFB-group bacterium MBIC04471.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=135551 {ECO:0000313|EMBL:BAB40402.1};
RN [1] {ECO:0000313|EMBL:BAB40402.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MBIC04471 {ECO:0000313|EMBL:BAB40402.1};
RA Suzuki M., Takadera T., Harayama S., Yamamoto S.;
RT "Diversity of marine Cytophaga-like bacteria: Phylogenetic analysis using
RT gyrB sequences and their carotenoids profiles.";
RL Submitted (AUG-2000) 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}.
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DR EMBL; AB047179; BAB40402.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AJI7; -.
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; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR CDD; cd03366; TOPRIM_TopoIIA_GyrB; 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 InterPro; IPR034160; TOPRIM_GyrB.
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; 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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 320..439
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAB40402.1"
FT NON_TER 474
FT /evidence="ECO:0000313|EMBL:BAB40402.1"
SQ SEQUENCE 474 AA; 52966 MW; 1D38EEF356D805BB CRC64;
DKDSYKVSGG LHGVGVSCVN ALSDHLKATV HRDGKIWEQE YERGKTLYPV KSVGETDITG
TIVTFVPDKS IFTQTVEYNY DTLANRMREL AYLNKGVTIT MTDKRNKDEK GEFIAETFFS
NEGLKEFIKF LDETREPLIQ SVISMEGEKN GIPVEVAMIY NTGFSENLHS YVNNINTHEG
GTHLSGFRRG LTSTLKKYAD SSGMLDKLKF EVSGDDFREG LTAIVSVKVA EPQFEGQTKT
KLGNREVTSA VSQAVSEMLT NYLEEHPDDA KSVVQKVILA AQARHAAAKA REMVQRKNPM
SVGGLPGKLS DCSEQDPTKC EVFLVEGDSA GGTAKQGRDR NFQAILPLRG KILNVEKAMQ
HKVFENEEIK NIYTALGVTI GTEEDSKALN LEKLRYHKVV IMCDADVDGS HIETLILTFF
FRYMRELIEG GHVYIATPPL YLVKKGAKRR YAWNDQERDE IVESMKGGAS IQRY
//
