ID M9P0P5_BACLI Unreviewed; 381 AA.
AC M9P0P5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:AFV52743.1};
OS Bacillus licheniformis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402 {ECO:0000313|EMBL:AFV52743.1};
RN [1] {ECO:0000313|EMBL:AFV52743.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y68a {ECO:0000313|EMBL:AFV52743.1};
RX PubMed=23571124; DOI=10.1016/j.ijfoodmicro.2013.02.008;
RA Agbobatinkpo P.B., Thorsen L., Nielsen D.S., Azokpota P., Akissoe N.,
RA Hounhouigan J.D., Jakobsen M.;
RT "Biodiversity of aerobic endospore-forming bacterial species occurring in
RT Yanyanku and Ikpiru, fermented seeds of Hibiscus sabdariffa used to produce
RT food condiments in Benin.";
RL Int. J. Food Microbiol. 163:231-238(2013).
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; JX513940; AFV52743.1; -; Genomic_DNA.
DR AlphaFoldDB; M9P0P5; -.
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 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: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 307..381
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFV52743.1"
FT NON_TER 381
FT /evidence="ECO:0000313|EMBL:AFV52743.1"
SQ SEQUENCE 381 AA; 42325 MW; 230602EA12C40F39 CRC64;
GLHGVGASVV NALSTELDVT VYRDGKVHYQ EFERGVPKAD LKVIGDTEVT GTTTHFKPDP
EIFTETTEYD YDTLATRVRE LAFLTKGVKI TIEDKREGKE RKNDYCYEGG IKSYVEHLNR
SREVVHEEPV YIEGSKDGIT VEVALQYNDS YTSNIYSFAN NIHTYEGGTH EAGFKTGLTR
VINDYARRNG VFKESDPNLS GEDVREGLTA IISIKHPDPQ FEGQTKTKLG NSEARTITDA
LFSEALEKFL LENPDSAKKI VEKGVMAARA RMAAKKAREL TRRKSALEVS NLPGKLADCS
SKDPTISELY IVEGDSAGGS AKQGRDRHFQ AILPLRGKIL NVEKARLDKI LSNNEVRSMI
TALGTGIGED FNLEKARYHK V
//