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Database: UniProt
Entry: D5MP28_9CYAN
LinkDB: D5MP28_9CYAN
Original site: D5MP28_9CYAN 
ID   D5MP28_9CYAN            Unreviewed;       352 AA.
AC   D5MP28;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:BAJ07434.1};
OS   Planktothrix mougeotii.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Planktothrix.
OX   NCBI_TaxID=54306 {ECO:0000313|EMBL:BAJ07434.1};
RN   [1] {ECO:0000313|EMBL:BAJ07434.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TR1 {ECO:0000313|EMBL:BAJ07434.1}, and TR2-4
RC   {ECO:0000313|EMBL:BAJ07435.1};
RA   Hamada T., Harayama S.;
RT   "Identification and Classification of Beta Proteobacteria.";
RL   Submitted (NOV-1998) 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; AB020285; BAJ07434.1; -; Genomic_DNA.
DR   EMBL; AB020286; BAJ07435.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5MP28; -.
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; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; 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   Pfam; PF02518; HATPase_c; 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.
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, ECO:0000313|EMBL:BAJ07434.1};
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          2..124
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAJ07434.1"
FT   NON_TER         352
FT                   /evidence="ECO:0000313|EMBL:BAJ07434.1"
SQ   SEQUENCE   352 AA;  38758 MW;  F5DF224ECF2C4DA0 CRC64;
     AGYCTHIEID FNADGSVTVT DDGRGIPVDT HSKTGKSALE TVLTVLHAGG KFGGGGYKVS
     GGLHGVGVSV VNALSEWVEV TVFRDKKEYR QRFERGTPVT ELTSKPIKEN RTGTSLRFFP
     DTVIFTSGIE FDCDTIASRL RELAYLNAGV KVTLTDNRLE LLKRETPRIE TYCYEGGIRE
     YIAYMNNDKQ PLHEDIIYIS GERSNVQIEV ALQWCTDAYS DTILGFANNI RTIDGGTHLE
     GLKTVLTRTL NTIARKRNKL KEGEANLGGE NIREGLTAVI SAKVPDPEFE GQTKTRLGNP
     EVRGIVDSLV GEALTEYLEF NPGIADAVIE KAIQAFKAAE AARRARDLVR RK
//
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