(data stored in SCRATCH9089 zone)

SWISSPROT: Q1MIV6_RHIL3

ID   Q1MIV6_RHIL3            Unreviewed;       751 AA.
AC   Q1MIV6;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   11-DEC-2019, entry version 98.
DE   RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00936};
DE   AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
GN   Name=parC {ECO:0000256|HAMAP-Rule:MF_00936,
GN   ECO:0000313|EMBL:CAK07104.1};
GN   OrderedLocusNames=RL1609 {ECO:0000313|EMBL:CAK07104.1};
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae;
OC   Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596 {ECO:0000313|EMBL:CAK07104.1, ECO:0000313|Proteomes:UP000006575};
RN   [1] {ECO:0000313|EMBL:CAK07104.1, ECO:0000313|Proteomes:UP000006575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841 {ECO:0000313|EMBL:CAK07104.1,
RC   ECO:0000313|Proteomes:UP000006575};
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach A.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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:0000256|HAMAP-
CC       Rule:MF_00936}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00936,
CC         ECO:0000256|SAAS:SAAS01218217};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC       Rule:MF_00936}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00936}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. ParC type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00936}.
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DR   EMBL; AM236080; CAK07104.1; -; Genomic_DNA.
DR   RefSeq; WP_011651291.1; NC_008380.1.
DR   STRING; 216596.RL1609; -.
DR   EnsemblBacteria; CAK07104; CAK07104; RL1609.
DR   KEGG; rle:RL1609; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076277; -.
DR   KO; K02621; -.
DR   OMA; PRSNRID; -.
DR   OrthoDB; 217468at2; -.
DR   Proteomes; UP000006575; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_00936; ParC_type1; 1.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR005742; TopoIV_A_Gneg.
DR   Pfam; PF03989; DNA_gyraseA_C; 3.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q1MIV6.
DR   SWISS-2DPAGE; Q1MIV6.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00936,
KW   ECO:0000256|SAAS:SAAS01062879};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00936, ECO:0000256|SAAS:SAAS00972514,
KW   ECO:0000313|EMBL:CAK07104.1}; Membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00936,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   DOMAIN          19..471
FT                   /note="TOP4c"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   ACT_SITE        130
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            50
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            86
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            88
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            129
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ   SEQUENCE   751 AA;  83644 MW;  AEF5655AD1D4B812 CRC64;
     MGQEILPPSG GDDDHIQPVD LKAALEQRYL AYALSTIMHR ALPDVRDGLK PVHRRIVYAM
     NEMGLRPNSA FRKCAKIVGE VMGNYHPHGD QSIYDALARL AQDFSQRYTL VNGQGNFGNI
     DGDSPAAMRY TESKMTAVSE LLLEGIDQDA VDFRDTYDES NSEPVVLPGA FPNLLANGSS
     GIAVGMATSI PSHNAHELCD AALHLIKHPD ATVEKLVEFI PGPDFPTGGI IIDNRESIIE
     SYRTGRGGFR VRAKWQTEDL GRGGYQIVIT EIPFQVQKSR LIEKIAELLI ARKLPLLEDI
     RDESAEDIRV VLVPKTRSVD PTILMESMFK LTELESRFPL NMNVLSMGRI PRVMALNEVL
     KEWLDHRREV LQRRSRFRLA AIDRRLEILS GLLVAYLNID EVIRIIREED EPKPVMMARW
     DLTDNQVEAI LNMRLRALRK LEEFEIRKEF DELTKEKGEI EALLSSDDKQ WQTVAWEIGE
     VKKKFAKATE VGRRRTQFAD APETDEEAIQ QAMIEKEPIT VVISEKGWIR ALKGHIADTA
     ALTFKEGDGL KIAFPAQTTD KILIVTTGGK AFTLGGDKLP GGRGHGEPLR IIVDMDNDQA
     VLTAFVHDPS RKQLIVSTAG NGFVVPEAEL VANTRKGKQI MNVGLPEETQ LLVPVSGDHV
     AVVGENRKLL VFPLAQVPEM SRGKGVRLQR YKDGGISDVR CFAISDGLVW EDSAGRTFTK
     SKDELVEWLA DRATAGRTVP KGFPRSGKFA G
//

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