ID A0A0D3CLH8_BRAOL Unreviewed; 730 AA.
AC A0A0D3CLH8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 39.
DE RecName: Full=DNA gyrase subunit B {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=106296101 {ECO:0000313|EnsemblPlants:Bo5g137640.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g137640.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo5g137640.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo5g137640.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded DNA in an ATP-dependent manner.
CC {ECO:0000256|RuleBase:RU362094}.
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 ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC breakage and rejoining; the B chain catalyzes ATP hydrolysis.
CC {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708, ECO:0000256|RuleBase:RU362094}.
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DR RefSeq; XP_013587612.1; XM_013732158.1.
DR AlphaFoldDB; A0A0D3CLH8; -.
DR STRING; 109376.A0A0D3CLH8; -.
DR EnsemblPlants; Bo5g137640.1; Bo5g137640.1; Bo5g137640.
DR GeneID; 106296101; -.
DR Gramene; Bo5g137640.1; Bo5g137640.1; Bo5g137640.
DR KEGG; boe:106296101; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_006146_4_1_1; -.
DR OMA; KIAYAWT; -.
DR OrthoDB; 231762at2759; -.
DR Proteomes; UP000032141; Chromosome C5.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
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 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:SF7; DNA GYRASE SUBUNIT B, CHLOROPLASTIC; 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, ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362094};
KW Transit peptide {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 511..618
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 730 AA; 81002 MW; E546BE7EE20BDA6D CRC64;
MALLQRPAPY LHFYFRLMAS RSRLFSHSLC PSLHRHSSSL SSSTPRIKFQ LAKVLSQRLV
IRNAVSPRSF MSSTMDTDAL HESSTSKDYS SEHIQVLEGL DPVRKRPGMY IGSTGSRGLH
HLVYEILDNA IDEAQAGFAS KIDVVLHADG SVSISDDGRG IPTDLHPATR KSSLETVLTV
LHAGGKFGGK SSGYSVSGGL HGVGLSVVNA LSEALEVIVR RDGMEFQHKY SRGKPITTLT
CHVLPPESRG TQGTCIRFWP DKEVFTTAIQ FDHNTIAGRI RELAFLNPKV TISLKKEDDD
PERDLYSEYF YAGGLTEYVS WLNTDKKPLH DVLGFRKEIN GTTVDVALQW CSDAYSDTML
GYANSIRTID GGTHIEGVKA SLTRTLNSLA KKLKVIKEKD ISLSGEHVRE GLTCIVSVKV
PDPEFEGQTK TRLGNPEVRK IVDQSLQEYL TEYLELHPDV LESIISKSLN AYKAALAAKR
ARELVRSKSI LKSSSLPGKL ADCSSTDPAE SEIFIVEGDS AGGSAKQGRD RRFQAILPLR
GKILNIERKD EAAMYKNEEI QNLILGLGLG VKGEDFNMEN LRYHKIIILT DADVDGAHIR
TLLLTFFFRY QRALFDAGCI YVGVPPLFKV ERGKQAHYCY DEAALKQVIA SFPGNASYNI
QRFKGLGEMM PEQLWETTMN PDTRILKQLV VDDAAETNVV FSSLMGARVD VRKELIKSAA
TRMNLENLDI
//