XERD_STAAU
ID XERD_STAAU Reviewed; 295 AA.
AC P0A0P2; O87666; Q9KJF7; Q9RGN6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WCUH29 / NCIMB 40771;
RX PubMed=10939248;
RA Chalker A.F., Lupas A., Ingraham K., So C.Y., Lunsford R.D., Li T.,
RA Bryant A., Holmes D.J., Marra A., Pearson S.C., Ray J., Burnham M.K.R.,
RA Palmer L.M., Biswas S., Zalacain M.;
RT "Genetic characterization of Gram-positive homologs of the XerCD site-
RT specific recombinases.";
RL J. Mol. Microbiol. Biotechnol. 2:225-233(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tichat N., Szatmari G.B.;
RT "Cloning and characterization of the Staphylococcus aureus xerD gene.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293.
RC STRAIN=RN450 8325-4;
RX PubMed=10746769; DOI=10.1099/00221287-146-3-659;
RA Xiong A., Singh V.K., Cabrera G., Jayaswal R.K.;
RT "Molecular characterization of the ferric-uptake regulator, Fur, from
RT Staphylococcus aureus.";
RL Microbiology 146:659-668(2000).
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}.
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DR EMBL; AF173869; AAF89876.1; -; Genomic_DNA.
DR EMBL; AF093548; AAC64162.1; -; Genomic_DNA.
DR EMBL; AF118839; AAF21314.1; -; Genomic_DNA.
DR RefSeq; WP_000447733.1; NZ_WYDB01000002.1.
DR AlphaFoldDB; P0A0P2; -.
DR SMR; P0A0P2; -.
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_0000095422"
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"
FT CONFLICT 237
FT /note="T -> K (in Ref. 1; AAF89876)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="R -> K (in Ref. 1; AAF89876)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..290
FT /note="NQ -> YP (in Ref. 1; AAF89876)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="P -> A (in Ref. 3; AAF21314)"
FT /evidence="ECO:0000305"
FT CONFLICT 294..295
FT /note="RA -> KT (in Ref. 1; AAF89876)"
FT /evidence="ECO:0000305"
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
