XERC1_RALSO
ID XERC1_RALSO Reviewed; 329 AA.
AC Q8Y3C8;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Tyrosine recombinase XerC 1;
GN Name=xerC1; OrderedLocusNames=RSc0052; ORFNames=RS01875;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC the cutting and rejoining of the recombining DNA molecules. The XerC-
CC XerD complex is essential to convert dimers of the bacterial chromosome
CC into monomers to permit their segregation at cell division. It also
CC contributes to the segregational stability of plasmids (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000305}.
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DR EMBL; AL646052; CAD13580.1; -; Genomic_DNA.
DR RefSeq; WP_011000019.1; NC_003295.1.
DR AlphaFoldDB; Q8Y3C8; -.
DR SMR; Q8Y3C8; -.
DR STRING; 267608.RSc0052; -.
DR EnsemblBacteria; CAD13580; CAD13580; RSc0052.
DR GeneID; 60499561; -.
DR KEGG; rso:RSc0052; -.
DR eggNOG; COG4973; Bacteria.
DR HOGENOM; CLU_027562_9_0_4; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.130; -; 1.
DR Gene3D; 1.10.443.10; -; 1.
DR HAMAP; MF_01808; Recomb_XerC_XerD; 1.
DR InterPro; IPR044068; CB.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013762; Integrase-like_cat_sf.
DR InterPro; IPR002104; Integrase_catalytic.
DR InterPro; IPR010998; Integrase_recombinase_N.
DR InterPro; IPR004107; Integrase_SAM-like_N.
DR InterPro; IPR011931; Recomb_XerC.
DR InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR Pfam; PF02899; Phage_int_SAM_1; 1.
DR Pfam; PF00589; Phage_integrase; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR TIGRFAMs; TIGR02224; recomb_XerC; 1.
DR PROSITE; PS51900; CB; 1.
DR PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA integration; DNA recombination; DNA-binding; Reference proteome.
FT CHAIN 1..329
FT /note="Tyrosine recombinase XerC 1"
FT /id="PRO_0000095318"
FT DOMAIN 14..101
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 123..320
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 163
FT /evidence="ECO:0000250"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT ACT_SITE 298
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 36008 MW; 1A344F941D27E177 CRC64;
MPPSAPDDDR DAPAPPHPQI GAYLDALKFE RKLSQHTLAS YARELAVLQQ LGARFAAGID
LMRLQPHHIR RMMAQLHGGG LSGRSIARAL SAWRGWYQWL ALRDAAVTAN PVDGIRAPKS
PKRLPKALSV EQAVALMEQL PGDDPEAVRD RAVNELFYSC GLRLSELVGL DLRHAQAGDY
ASASWLDLEA REVTVLGKGN KRRTVPVGSK AAEALAAWLA VRPQLAQPDA APEDAHALFL
SARGKRLAQR QIQTRMKRNA IAAGVPADVH PHVLRHSFAT HMLQSSGDLR AVQELLGHAS
IASTQVYTSL DFQHLAKIYD QAHPRAKKK