ID B1V9B6_PHYAS Unreviewed; 662 AA.
AC B1V9B6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=gyrB {ECO:0000313|EMBL:CAM11548.1};
GN OrderedLocusNames=PA0213 {ECO:0000313|EMBL:CAM11548.1};
OS Phytoplasma australiense.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrXII (Stolbur group).
OX NCBI_TaxID=59748 {ECO:0000313|EMBL:CAM11548.1, ECO:0000313|Proteomes:UP000008323};
RN [1] {ECO:0000313|EMBL:CAM11548.1, ECO:0000313|Proteomes:UP000008323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18359806; DOI=10.1128/JB.01301-07;
RA Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT and AY-WB.";
RL J. Bacteriol. 190:3979-3991(2008).
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; AM422018; CAM11548.1; -; Genomic_DNA.
DR AlphaFoldDB; B1V9B6; -.
DR STRING; 59748.PA0213; -.
DR KEGG; pal:PA0213; -.
DR eggNOG; COG0187; Bacteria.
DR Proteomes; UP000008323; Chromosome.
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 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000008323};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 435..553
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 662 AA; 74823 MW; 4844B6016E5C9577 CRC64;
MKNYNADSIQ ILEGLEAVRK RPGMYIGSTA AKGLHHLVWE IVDNSIDEAL AGHANEITLE
ILPGDIISVT DNGRGIPVGI HHKTGKPAVE TILTTLHAGG KFDSSSYKIS GGLHGVGASV
VNALSSWFSV EIHLDKKIHY QKYEKGVPVA PLEVIGKTDR KGTVIKFLAD PSIFQETTIY
DAKILKERIQ QLSFLNKGLK LNLIDQRQEK PVSFNFYHEK GLQDYLTFIN QTYMQKPFHN
LFVLEKELDN LALEIVFEYT VNDDEKSKQQ EEEQAIKNYT QTQKIYSFVN NIHTHEGGTH
EEGFKLALSR NFSKYAKDYN LLKKNESLLS EDILEGITAI ISLKHQDPQF EGQTKAKLGN
VEVRQIVSQY FGEALGRFLL ENPGDAKKII EKCLLSANAR LAAKRAREIV RNKPLDTLGF
AAKLADCRSK DPKISELYIV EGDSAGGSAK QGRDSHFQAI LPLKGKVLNV EKTQSSKILT
NKEIKSLIQA IGIGVDINKQ KNLNLDKLRY HKIIIMTDAD VDGAHIRTLL LTFFFRNLRI
LIEKGYIYFA RPPLYKYQKG KNITYFYEEK EKIDFSLKKN IKDGFQRYKG LGEMNPDQLW
ETTMNPEKRT LLQASLKDAL NALSDEEAIK EANSTFNILM GKEVFPRKEF ILNNALEADL
DV
//
