ID   XERD_STAAS              Reviewed;         295 AA.
AC   Q6G967;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN   Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; OrderedLocusNames=SAS1437;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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_01807}.
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_01807}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01807}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01807}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571857; CAG43214.1; -; Genomic_DNA.
DR   RefSeq; WP_000447733.1; NC_002953.3.
DR   AlphaFoldDB; Q6G967; -.
DR   SMR; Q6G967; -.
DR   KEGG; sas:SAS1437; -.
DR   HOGENOM; CLU_027562_9_6_9; -.
DR   OMA; HSFASHM; -.
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   HAMAP; MF_01807; Recomb_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; IPR011932; Recomb_XerD.
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; TIGR02225; recomb_XerD; 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..295
FT                   /note="Tyrosine recombinase XerD"
FT                   /id="PRO_0000095420"
FT   DOMAIN          1..85
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          106..289
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        276
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ   SEQUENCE   295 AA;  34133 MW;  4AA14322A9D8D156 CRC64;
     METIIEEYLR FIQIEKGLSS NTIGAYRRDL KKYQDYMTEH HISHIDFIDR QLIQECLGHL
     IDQGQSAKSI ARFISTIRSF HQFAIREKYA AKDPTVLLDS PKYDKKLPDV LNVDEVLALL
     ETPDLNKING YRDRTMLELL YATGMRVSEL IHLELENVNL IMGFVRVFGK GDKERIVPLG
     DAVIEYLTTY IETIRPQLLK KTVTEVLFLN MHGKPLSRQA IWKMIKQNGV KANIKKTLTP
     HTLRHSFATH LLENGADLRA VQEMLGHSDI STTQLYTHVS KSQIRKMYNQ FHPRA