ID A8R237_9CHRO Unreviewed; 138 AA.
AC A8R237;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 43.
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:BAF92310.1};
OS Microcystis ichthyoblabe TAC146.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=449515 {ECO:0000313|EMBL:BAF92310.1};
RN [1] {ECO:0000313|EMBL:BAF92310.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TAC146 {ECO:0000313|EMBL:BAF92310.1};
RA Tanabe Y., Kasai F., Watanabe M.M.;
RT "Multilocus sequence typing (MLST) reveals high genetic diversity and
RT clonal population structure of the toxic cyanobacterium Microcystis
RT aeruginosa.";
RL Microbiology (Mosc.) 153:3695-3703(2007).
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; AB325131; BAF92310.1; -; Genomic_DNA.
DR AlphaFoldDB; A8R237; -.
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 27..138
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAF92310.1"
FT NON_TER 138
FT /evidence="ECO:0000313|EMBL:BAF92310.1"
SQ SEQUENCE 138 AA; 15532 MW; 633B7E5B14733F0B CRC64;
LNAGVKITFS DYRPEEPHIE TYCYEGGIKE YVAYMCREKE TLHKDIIYVS GEKTGINIEV
AFQWCIDAYS DNILGFANNI RTIDGGTHLE GLKAVLTRTL NNVARKRNKI KENEPNLAGE
NVREGLTAVI SVKVPEPE
//
