PARE_MYCCT
ID PARE_MYCCT Reviewed; 643 AA.
AC P50028; Q2SS32;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000305};
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=Topoisomerase IV subunit B;
GN Name=parE; Synonyms=gyrB {ECO:0000303|PubMed:7828871};
GN OrderedLocusNames=MCAP_0457;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7828871; DOI=10.1016/0378-1119(94)90653-x;
RA Sano K., Miyata M.;
RT "The gyrB gene lies opposite from the replication origin on the circular
RT chromosome of Mycoplasma capricolum.";
RL Gene 151:181-183(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000250|UniProtKB:Q59961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
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|PROSITE-
CC ProRule:PRU00995};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE.
CC {ECO:0000250|UniProtKB:Q59961}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: There is a bona fide GyrB elsewhere in this organism
CC (UniProtKB:Q2ST75). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; D28808; BAA05969.1; -; Genomic_DNA.
DR EMBL; D21231; BAA04763.1; -; Genomic_DNA.
DR EMBL; D26016; BAA05031.1; -; Genomic_DNA.
DR EMBL; CP000123; ABC01260.1; -; Genomic_DNA.
DR RefSeq; WP_011387330.1; NC_007633.1.
DR AlphaFoldDB; P50028; -.
DR SMR; P50028; -.
DR EnsemblBacteria; ABC01260; ABC01260; MCAP_0457.
DR GeneID; 23778587; -.
DR KEGG; mcp:MCAP_0457; -.
DR HOGENOM; CLU_006146_4_1_14; -.
DR OMA; KIAYAWT; -.
DR OrthoDB; 205481at2; -.
DR Proteomes; UP000001928; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 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; Cytoplasm; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Topoisomerase.
FT CHAIN 1..643
FT /note="DNA topoisomerase 4 subunit B"
FT /id="PRO_0000145317"
FT DOMAIN 420..534
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
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|PROSITE-ProRule:PRU00995"
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|PROSITE-ProRule:PRU00995"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 451
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 454
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT CONFLICT 392
FT /note="I -> V (in Ref. 1; BAA04763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 72352 MW; E1EDBDC92BA8AAAB CRC64;
MAENKKYDES AIQVLEGLEA VRKRPGMYIG STDNKGLHHL VWEIVDNAID EALAGYCTQI
DVILEKDNSI TVIDNGRGIP TGMHKTGKPT PEVIFSVLHA GGKFDSTAYK SSGGLHGVGS
SVTNALSKRF KAIIYRDKKI HEIEFKNGGK LEKPLTFINT TYKTGTTINF LPDDTIFSNA
KFNFSLISER LKESALLNSG LKITLSDLIS NRYVEYQFQD GLVEFVKELV DDKTPVTDII
TINNESKNII VEIALQYTED DNEIILGFAN NVKTIDGGTH LVGFKSGLIR AINDYAKDQK
ILKDKTKLDS NDLREGLVAI VTVKIPENLI EYEGQTKSKL GTSDAKTVVE QIVYEFMSYW
LIENKVLANK VIENALNAQK ARIAAKQARQ AIKSVKGKKN VNKLMLGKLT PAQGKKRELN
ELYLVEGDSA GGSAKSGRDR NFQAILPLRG KVINSEKAKL VDLLKNEEIQ SIINAIGAGV
GKDFDISDIN YGKIIIMTDA DTDGAHIQTL LLTFFYRHMK DLIIHKKVYI ALPPLYKITF
NDKSFIYLWD EEELNKFNKT NTKKYEIQRY KGLGEMNADQ LWQTTMDPKN RKIIQVTISD
GLLAERMFKT LMGDDVEKRK LWIQENVKFT LEDDQIQIIE MEK