ID Q6WXL4_BACTU Unreviewed; 99 AA.
AC Q6WXL4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:AAP88097.1};
OS Bacillus thuringiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1428 {ECO:0000313|EMBL:AAP88097.1};
RN [1] {ECO:0000313|EMBL:AAP88097.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMSNU 10051 {ECO:0000313|EMBL:AAP88098.1}, IMSNU 11043
RC {ECO:0000313|EMBL:AAP88100.1}, IMSNU 12087
RC {ECO:0000313|EMBL:AAP88103.1}, IMSNU 12088
RC {ECO:0000313|EMBL:AAP88104.1}, IMSNU 12089
RC {ECO:0000313|EMBL:AAP88097.1}, IMSNU 12090
RC {ECO:0000313|EMBL:AAP88101.1}, IMSNU 12091
RC {ECO:0000313|EMBL:AAP88102.1}, IMSNU 12093
RC {ECO:0000313|EMBL:AAP88105.1}, IMSNU 12096
RC {ECO:0000313|EMBL:AAP88099.1}, and KCTC 1509
RC {ECO:0000313|EMBL:AAP88096.1};
RX PubMed=15322020; DOI=10.1128/IAI.72.9.5253-5261.2004;
RA Ko K.S., Kim J.W., Kim J.M., Kim W., Chung S.I., Kim I.J., Kook Y.H.;
RT "Population structure of the Bacillus cereus group as determined by
RT sequence analysis of six housekeeping genes and the plcR Gene.";
RL Infect. Immun. 72:5253-5261(2004).
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; AY265502; AAP88096.1; -; Genomic_DNA.
DR EMBL; AY265503; AAP88097.1; -; Genomic_DNA.
DR EMBL; AY265504; AAP88098.1; -; Genomic_DNA.
DR EMBL; AY265505; AAP88099.1; -; Genomic_DNA.
DR EMBL; AY265506; AAP88100.1; -; Genomic_DNA.
DR EMBL; AY265507; AAP88101.1; -; Genomic_DNA.
DR EMBL; AY265508; AAP88102.1; -; Genomic_DNA.
DR EMBL; AY265509; AAP88103.1; -; Genomic_DNA.
DR EMBL; AY265510; AAP88104.1; -; Genomic_DNA.
DR EMBL; AY265511; AAP88105.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WXL4; -.
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 Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
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 PRINTS; PR01159; DNAGYRASEB.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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 2..99
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP88097.1"
FT NON_TER 99
FT /evidence="ECO:0000313|EMBL:AAP88097.1"
SQ SEQUENCE 99 AA; 11014 MW; 01D35E4EF3787149 CRC64;
PVYVEGSKDG IQVEVALQYN EGYTNHIYSF TNNIHTYEGG THEVGFKTAL TRVINDYGRK
NNILKDADSN LTGEDVREGL TAIVSIKHPN PQFEGLTKT
//
