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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
 
 
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