(data stored in SCRATCH3701 zone)

SWISSPROT: PARC_RICTY

ID   PARC_RICTY              Reviewed;         737 AA.
AC   Q68XU1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 98.
DE   RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00936};
DE   AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
GN   Name=parC {ECO:0000255|HAMAP-Rule:MF_00936}; OrderedLocusNames=RT0065;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00936};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP-
CC       Rule:MF_00936}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00936};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00936}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. ParC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00936}.
DR   EMBL; AE017197; AAU03551.1; -; Genomic_DNA.
DR   RefSeq; WP_011190538.1; NC_006142.1.
DR   SMR; Q68XU1; -.
DR   STRING; 257363.RT0065; -.
DR   PRIDE; Q68XU1; -.
DR   EnsemblBacteria; AAU03551; AAU03551; RT0065.
DR   KEGG; rty:RT0065; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076277; -.
DR   KO; K02621; -.
DR   OMA; PRSNRID; -.
DR   OrthoDB; 217468at2; -.
DR   BioCyc; RTYP257363:G1G0L-66-MONOMER; -.
DR   Proteomes; UP000000604; 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; Q68XU1.
DR   SWISS-2DPAGE; Q68XU1.
KW   Cell membrane; DNA-binding; Isomerase; Membrane; Topoisomerase.
FT   CHAIN           1..737
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000273115"
FT   ACT_SITE        120
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            40
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            76
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            78
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            119
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
SQ   SEQUENCE   737 AA;  83414 MW;  CF736359974EBB90 CRC64;
     MKEAKIENID FGNALSERYL AYALSTIMSR SLPDVRDGLK PVHRRLLYAM LQLRLEPNSG
     YKKCARVVGD VIGKYHPHGD VAVYDTLVRL AQHFSLRYPL IDGQGNFGSI DGDNAAAMRY
     TESRMTEICM LLMKDIDKDT VDFRSTYDDS DLEPVIMPAS FPNLLANGSE GIAVGMATNI
     PPHNLHELCD ALLYLIDNPQ AGVNDIMNFI KGPDFPTGGI IIDQTKVINA AYTTGRGSFR
     VRSRWEKEEL SYGTYQIVVT EIPYQVQKSK LIEQIAILLK DKKIPLISSI RDESTDIIRL
     VIEPRDRSCD PQIVMESLFK LTNLESRIQL NMNVIGSNNV PRVMNIVEIL QEFLVHRQNI
     ITRRSTYLLN KIKQRLEILK VLKIVYLNLD EIIEIIRRED EPKTIIMERF KISEIQVEVI
     LNTRLRALQK LEEHAIIDEH SNLQKQQAIL EKILKNHKEL WKIVKKEIKS VQTQFGLNTI
     IGARRTSFEE VDLTNQVIDI TAFITKEPIT IICSKMGWIR LLKGHNTDLS TIKYKEGDAE
     KFIIEAYTTD KILIISSKGR FFTLLADNIS KGKGTAVSIK LLVDIGNNDI TNILVYKPYQ
     LLLLASSIGK GFLVNSNEVI AQTKAGKQIM NIPEGYACIT CLPVNGNSIA CINESRRLLI
     FNINEIPEMK KGQGVVLQRF KNAKLLDIKI FNKEDGLSWN DGKKIQLEKN IVAFLGKRGS
     AGTLPPIGFP KNNRFSS
//

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