(data stored in SCRATCH zone)

SWISSPROT: C5B6Y3_EDWI9

ID   C5B6Y3_EDWI9            Unreviewed;       631 AA.
AC   C5B6Y3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_00938};
DE   AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
GN   Name=parE {ECO:0000256|HAMAP-Rule:MF_00938};
GN   OrderedLocusNames=NT01EI_0202 {ECO:0000313|EMBL:ACR67445.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67445.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Topoisomerase IV is essential for chromosome
CC       segregation. It relaxes supercoiled DNA. Performs the decatenation
CC       events required during the replication of a circular DNA molecule.
CC       {ECO:0000256|HAMAP-Rule:MF_00938}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_00938,
CC       ECO:0000256|SAAS:SAAS00470725}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00609977};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE.
CC       {ECO:0000256|HAMAP-Rule:MF_00938}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type
CC       1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00938}.
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DR   EMBL; CP001600; ACR67445.1; -; Genomic_DNA.
DR   RefSeq; WP_015869656.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0202; -.
DR   EnsemblBacteria; ACR67445; ACR67445; NT01EI_0202.
DR   GeneID; 7958790; -.
DR   KEGG; eic:NT01EI_0202; -.
DR   PATRIC; fig|634503.3.peg.179; -.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   HOGENOM; HOG000075154; -.
DR   KO; K02622; -.
DR   OMA; AKPNIMR; -.
DR   OrthoDB; POG091H03L6; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   HAMAP; MF_00938; ParE_type1; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR003594; HATPase_C.
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.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR013759; Topo_IIA_cen_dom.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR005737; TopoIV_B_Gneg.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   PANTHER; PTHR10169; PTHR10169; 1.
DR   PANTHER; PTHR10169:SF59; PTHR10169:SF59; 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; PR00418; TPI2FAMILY.
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; TIGR01055; parE_Gneg; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B6Y3.
DR   SWISS-2DPAGE; C5B6Y3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00938,
KW   ECO:0000256|SAAS:SAAS00528655};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00938};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00938,
KW   ECO:0000256|SAAS:SAAS00107007, ECO:0000313|EMBL:ACR67445.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00938,
KW   ECO:0000256|SAAS:SAAS00528653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00938,
KW   ECO:0000256|SAAS:SAAS00528650}.
FT   DOMAIN      413    526       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   NP_BIND     111    117       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   BINDING       6      6       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   BINDING      43     43       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   BINDING      70     70       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   BINDING     335    335       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   SITE        447    447       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00938}.
FT   SITE        498    498       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00938}.
FT   SITE        616    616       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00938}.
SQ   SEQUENCE   631 AA;  70103 MW;  C6AC320083428E61 CRC64;
     MTQSSYNADA IEVLSGLEPV RRRPGMYTDT TRPNHLGQEV IDNSVDEALA GHATRIEVIL
     HPDQSLEVID NGRGMPVDIH PEEGVPAIEL ILCRLHAGGK FSNKNYQFSG GLHGVGISVV
     NALSRRVEVS VRRDGQIYQM AFENGEKVED LHVSGTVGRR NTGTSVHFWP DAQFFDSARF
     SVSRLTHLLK AKAVLCPGVE ILFRDLVNGS EQRWCYQDGL TDYLMESVNG LVTLPEQPFT
     GTFASDTEAV DWALLWLPEG GELLTESYVN LIPTPQGGTH VNGLRQGLLD AMREFCEFRN
     LLPRGVKLTA DDIWERCAYV LSVKMQDPQF AGQTKERLSS RQCAAFVSGV VKDAFSLWLN
     QNVQSAELLA ELAINSAQRR MRAAKKVVRK KLTSGPALPG KLADCSAQDL NRTELFLVEG
     DSAGGSAKQA RDREYQAIMP LKGKILNTWE VSSDEVLASQ EVHDISVAIG IDPDSDDLSQ
     LRYGKVCILA DADSDGLHIA TLLCALFVRH FRPLVQAGHV YVAMPPLYRI DLGKEVFYAL
     SEEEKAGVLE QLKRKKGKPN VQRFKGLGEM NPLQLRETTL DPNTRRLVQL AIEDEDMERT
     VAVMDMLLAK KRAEDRRNWL QENGNLAELD V
//

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