XERC_STACT
ID XERC_STACT Reviewed; 296 AA.
AC B9DPG4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=Sca_0886;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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.
CC {ECO:0000255|HAMAP-Rule:MF_01808}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD. {ECO:0000255|HAMAP-
CC Rule:MF_01808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01808}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01808}.
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DR EMBL; AM295250; CAL27796.1; -; Genomic_DNA.
DR RefSeq; WP_015900137.1; NC_012121.1.
DR AlphaFoldDB; B9DPG4; -.
DR SMR; B9DPG4; -.
DR STRING; 396513.SCA_0886; -.
DR GeneID; 60545418; -.
DR KEGG; sca:SCA_0886; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_9; -.
DR OMA; QAFWYLI; -.
DR OrthoDB; 745068at2; -.
DR BioCyc; SCAR396513:SCA_RS04475-MON; -.
DR Proteomes; UP000000444; 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.
FT CHAIN 1..296
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000187615"
FT DOMAIN 1..84
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 105..286
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 145
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 169
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 238
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 241
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 273
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 296 AA; 34744 MW; A5AFAFBAF3DD91E2 CRC64;
MNKIQESFLY MLKVERFFSK HTLKSYHDDL VQFNAFLEHE HLKLKSFEYK DARNYLSFLY
SKGLKRTTVS RKISTLRSFY EFWMTQDDTV VNPFVQLVHP KKEQYLPHFF YEEEMSALFE
TVEADGHKGL RDRVILELLY GTGIRVSELV NIKLEDLDLN SPGVKVLGKG NKERFIPFGN
MCRESIERYL ELFPPIQNVK HDYLLVNING RPITERGVRY VLNDIVKRTA GVTDIHPHKL
RHTFATHMLN EGADLRTVQS LLGHVNLSTT GRYTHVSNQQ LRKVYLNAHP RAKKEK