(data stored in ACNUC7421 zone)

SWISSPROT: Q3KJ13_PSEPF

ID   Q3KJ13_PSEPF            Unreviewed;       635 AA.
AC   Q3KJ13;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 116.
DE   RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
DE            EC=5.6.2.3 {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=Pfl01_0499 {ECO:0000313|EMBL:ABA72243.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72243.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72243.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72243.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00938, ECO:0000256|SAAS:SAAS01180974};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00924966};
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; CP000094; ABA72243.1; -; Genomic_DNA.
DR   RefSeq; WP_011332163.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0499; -.
DR   EnsemblBacteria; ABA72243; ABA72243; Pfl01_0499.
DR   KEGG; pfo:Pfl01_0499; -.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   HOGENOM; HOG000075154; -.
DR   KO; K02622; -.
DR   OMA; LADCAGQ; -.
DR   BioCyc; PFLU205922:G1G4S-504-MONOMER; -.
DR   Proteomes; UP000002704; 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 (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00075; HATPase_c; 1.
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; IPR036890; HATPase_C_sf.
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; IPR005737; TopoIV_B_Gneg.
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; TIGR01055; parE_Gneg; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJ13.
DR   SWISS-2DPAGE; Q3KJ13.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00938,
KW   ECO:0000256|SAAS:SAAS00924926};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00938};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00938,
KW   ECO:0000256|SAAS:SAAS00924998, ECO:0000313|EMBL:ABA72243.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00938,
KW   ECO:0000256|SAAS:SAAS00924952};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00938,
KW   ECO:0000256|SAAS:SAAS00924964}.
FT   DOMAIN      416    529       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   NP_BIND     114    120       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   BINDING       9      9       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   BINDING      46     46       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   BINDING      73     73       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   BINDING     338    338       ATP. {ECO:0000256|HAMAP-Rule:MF_00938}.
FT   SITE        450    450       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00938}.
FT   SITE        501    501       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00938}.
FT   SITE        620    620       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00938}.
SQ   SEQUENCE   635 AA;  69461 MW;  872C9A88DABD2905 CRC64;
     MATPSASSYN ADAIEVLSGL DPVRKRPGMY TDTSRPNHLA QEVIDNSVDE ALAGHAKSIQ
     VILHADHSLE VCDDGRGMPV DIHPEEGVSG VELILTKLHA GGKFSNKNYQ FSGGLHGVGI
     SVVNALSTQV RVRVKRDGNE YEMTFADGFK ATDLQVIGTV GKRNTGTSVY FAPDPKYFDS
     PKFSISRLKH VLKAKAVLCP GLLISFEDKG TGEKVEWHYE DGLRSYLVDA VSEFERLPDA
     PFCGNLAGTK EAVEWALLWL PEGGTSVTES YVNLIPTEQG GTHVNGLRQG LLDAMREFCE
     FRSLLPRGVK LAPEDVWERI AFVLSMKMQE PQFSGQTKER LSSREAAAFV SGVVKDAFSL
     WLNANPETGL ALAELAISNA GRRLKASKKV ERKRITQGPA LPGKLADCAG QDPMRSELFL
     VEGDSAGGSA KQARDKEFQA ILPLRGKILN TWEVDGSEVL ASQEVHNIAV AIGVDPGAED
     MSQLRYGKIC ILADADSDGL HIATLLCALF VQHFRPLVDA GHVYVAMPPL YRIDLGKEIY
     YALDEAERDG ILDRLVAEKK RGKPQVTRFK GLGEMNPPQL RETTMDPNTR RLVQLTLGGD
     FAETSEMMDM LLAKKRAGDR KTWLESKGNL AEVLA
//

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