ID B3VL58_BACTU Unreviewed; 627 AA.
AC B3VL58;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 08-NOV-2023, entry version 83.
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:ACE95120.1};
OS Bacillus thuringiensis serovar canadensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=180855 {ECO:0000313|EMBL:ACE95120.1};
RN [1] {ECO:0000313|EMBL:ACE95120.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IEBC-T05A001 {ECO:0000313|EMBL:ACE95120.1};
RA Soufiane B., Cote J.-C.;
RT "Relationships between Bacillus thuringiensis and the Bacillus cereus group
RT sensu lato inferred from 16S rRNA, gyrB and aroE gene sequence analyses.";
RL Submitted (MAY-2008) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; EU761180; ACE95120.1; -; Genomic_DNA.
DR AlphaFoldDB; B3VL58; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd16928; HATPase_GyrB-like; 1.
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 HAMAP; MF_01898; GyrB; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR011557; GyrB.
DR InterPro; IPR003594; HATPase_C.
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 NCBIfam; TIGR01059; gyrB; 1.
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; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 417..531
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACE95120.1"
FT NON_TER 627
FT /evidence="ECO:0000313|EMBL:ACE95120.1"
SQ SEQUENCE 627 AA; 70246 MW; 0D14A1E4AA7C7553 CRC64;
ENAYDESQIQ VLEGLEAVRK RPGMYIGSTS GKGLHHLVWE IVDNSIDEAL AGYCDEINVS
IEEDNSIRVT DNGRGIPVGI QEKMGRPAVE VIMTVLHAGG KFGGGGYKVS GGLHGVGASV
VNALSTELEV FVHREGKIHY QKYERGIPVA DLKVIGDTDQ TGTITRFKPD PEIFQETTVY
DFDTLATRMR ELAFLNRNIK LTIEDKREHK QKKEFHYEGG IKSYVEHLNR SKQPIHEEPV
YVEGSKDGIQ VEVSLQYNEG YTNNIYSFTN NIHTYEGGTH EVGFKTALTR VINDYGRKNS
ILKDADSNLT GEDVREGLTA IVSIKHPNPQ FEGQTKTKLG NSEARTITES VFSEAFEKFL
LENPNVARKI VEKGTMAARA RVAAKKAREL TRRKSALEVS SLPGKLADCS SKDPAISEIY
IVEGDSAGGS AKQGRDRHFQ AILPLKGKII NVEKARLDKI LSNDEVRTII TAIGTNIGGD
FDIEKARYHK VIIMTDADVD GAHIRTLLLT FFYRYMRQII ECGYIYIAQP PLFKIQQGKK
IQYAYNDKEL EKILAELPAQ PKPGIQRYKG LGEMNPTQLW ETTMDPEVRS LLQVSLQDAI
EADETFEILM GDKVEPRRNF IQENAKY
//
