PARE_MYCGA
ID PARE_MYCGA Reviewed; 633 AA.
AC Q59526;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000255|HAMAP-Rule:MF_00939};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00939};
DE AltName: Full=Topoisomerase IV subunit B {ECO:0000255|HAMAP-Rule:MF_00939};
GN Name=parE {ECO:0000255|HAMAP-Rule:MF_00939}; OrderedLocusNames=MYCGA4200;
GN ORFNames=MGA_0060;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RX PubMed=7783737;
RA Skamrov A.V., Feoktistova E.S., Bibilashvili R.S.;
RT "Cloning and analysis of the nucleotide sequence of the segment in the
RT Mycoplasma gallisepticum genome containing the gene for the ATP-binding
RT subunit of DNA topoisomerase type II (topIIB).";
RL Mol. Biol. (Mosk.) 29:308-316(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
CC -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It
CC relaxes supercoiled DNA. Performs the decatenation events required
CC during the replication of a circular DNA molecule. {ECO:0000255|HAMAP-
CC Rule:MF_00939}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00939};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|HAMAP-Rule:MF_00939};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP-
CC Rule:MF_00939}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00939}.
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DR EMBL; L35044; AAA91333.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56770.2; -; Genomic_DNA.
DR RefSeq; WP_011113666.1; NC_004829.2.
DR AlphaFoldDB; Q59526; -.
DR SMR; Q59526; -.
DR KEGG; mga:MGA_0060; -.
DR PATRIC; fig|233150.7.peg.470; -.
DR HOGENOM; CLU_006146_4_1_14; -.
DR OMA; KIAYAWT; -.
DR OrthoDB; 205481at2; -.
DR Proteomes; UP000001418; Chromosome.
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-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR HAMAP; MF_00939; ParE_type2; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005740; ParE_type2.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
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 Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR TIGRFAMs; TIGR01058; parE_Gpos; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..633
FT /note="DNA topoisomerase 4 subunit B"
FT /id="PRO_0000145431"
FT DOMAIN 420..534
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 5
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 113..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 426
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT SITE 451
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT SITE 454
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT SITE 506
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT SITE 619
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00939"
FT CONFLICT 157
FT /note="V -> M (in Ref. 1; AAA91333)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="N -> S (in Ref. 1; AAA91333)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="V -> I (in Ref. 1; AAA91333)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="S -> T (in Ref. 1; AAA91333)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="S -> T (in Ref. 1; AAA91333)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 71373 MW; 6DF59F0FBC1DA155 CRC64;
MVSNYNEKHI KVLKGLEPVR KRPGMYIGST DTRGLHHLVW ELFDNAVDEA LNGSANKIEV
VHKKDGSIIV TDNGRGIPVG KNLATNLSTV DTVYTVLHAG GKFDDQAYKV SGGLHGVGAS
VVNALSRKLI VTVHRDGGMY ESIYQDGGKI IQPLKKVGNS TKHGTIVQFW PDPTIFKNIQ
FNPYMIKERL HESSFLFKGL KIVFVDENNP ELSQTFIAKD GILEYLKYVN ENKKSISKII
PFKGDYEKIV VDGCFQYTDN ESELIISFAN SVKTSEGGSH ENGFKQAMLE TINDYSKKYK
LINNKDKGFD WSDLKEGLSV VLSVQVPEKI IAYEGQTKNK LFTQEVKVAV AKILTQQLFY
FLEENQADAK QLIERFKLIK EAKEAAKKAK ENTKKLKSAK SERVLYGKLT PAQQKNPLQN
EIFLVEGDSA GGTAKSGRDK RFQAILPLRG KVVNVEKSRL QDLLKNEEIL SIISCLGCGI
GNNFNIKNLK YHKIIIMTDA DTDGAHIQVL LLTFFYRYMK ELIEQGKVYI ALAPLYKISA
KNSNKSAFAW DDYQLDELRT KYGSYEVQRY KGLGEMNSEQ LWTTTMDPSK RQLIQVSIQN
AAQAERKVSI LMGDDASIRK NWINENVDFS IEE
