ID   XERC_STAA1              Reviewed;         298 AA.
AC   A7X1M7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=SAHV_1242;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF78125.1; -; Genomic_DNA.
DR   RefSeq; WP_001015601.1; NC_009782.1.
DR   AlphaFoldDB; A7X1M7; -.
DR   SMR; A7X1M7; -.
DR   KEGG; saw:SAHV_1242; -.
DR   HOGENOM; CLU_027562_9_0_9; -.
DR   OMA; QAFWYLI; -.
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..298
FT                   /note="Tyrosine recombinase XerC"
FT                   /id="PRO_1000070043"
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   298 AA;  35154 MW;  3DB376E2CAD4A5E3 CRC64;
     MNHIQEAFLN TLKVERNFSE HTLKSYQDDL IQFNQFLEQE HLQLKTFEYR DARNYLSYLY
     SNHLKRTSVS RKISTLRTFY EYWMTLDENI INPFVQLVHP KKEKYLPQFF YEEEMEALFK
     TVEEDTSKNL RDRVILELLY ATGIRVSELV NIKKQDIDFY ANGVTVLGKG SKERFVPFGA
     YCRQSIENYL EHFKPIQSCN HDFLILNMKG EAITERGVRY VLNDIVKRTA GVSEIHPHKL
     RHTFATHLLN QGADLRTVQS LLGHVNLSTT GKYTHVSNQQ LRKVYLNAHP RAKKENET