ID V5TEK5_CLOBO Unreviewed; 147 AA.
AC V5TEK5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:AHB62576.1};
OS Clostridium botulinum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1491 {ECO:0000313|EMBL:AHB62576.1};
RN [1] {ECO:0000313|EMBL:AHB62576.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CIP60.10B {ECO:0000313|EMBL:AHB62576.1};
RX PubMed=24246230;
RA Olsen J.S., Scholz H., Fillo S., Ramisse V., Lista F., Tromborg A.K.,
RA Aarskaug T., Thrane I., Blatny J.M.;
RT "Analysis of the genetic distribution among members of Clostridium
RT botulinum group I using a novel multilocus sequence typing (MLST) assay.";
RL J. Microbiol. Methods 96C:84-91(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; KF501780; AHB62576.1; -; Genomic_DNA.
DR AlphaFoldDB; V5TEK5; -.
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 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; 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; 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 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 69..147
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHB62576.1"
FT NON_TER 147
FT /evidence="ECO:0000313|EMBL:AHB62576.1"
SQ SEQUENCE 147 AA; 16112 MW; 5DD5FCADBA0EA3F0 CRC64;
DTIVGQSIGS FLEENPNVGK IIIEKGLSAS RAREAAKRAR ELTRRKSVLE STSLPGKLSD
CSSKDPSLCE IYLVEGDSAG GSAKQGRNRE FQAILPLKGK IMNVEKQRLD KILASDEIRA
MITAFGAGIG KEFDIDKIRY NRIIIMT
//
