XERD_XANCP
ID XERD_XANCP Reviewed; 323 AA.
AC Q8PCQ9;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; OrderedLocusNames=XCC0654;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(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.
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; AE008922; AAM39970.1; -; Genomic_DNA.
DR RefSeq; NP_636046.1; NC_003902.1.
DR RefSeq; WP_011035895.1; NC_003902.1.
DR AlphaFoldDB; Q8PCQ9; -.
DR SMR; Q8PCQ9; -.
DR STRING; 340.xcc-b100_3700; -.
DR EnsemblBacteria; AAM39970; AAM39970; XCC0654.
DR KEGG; xcc:XCC0654; -.
DR PATRIC; fig|190485.4.peg.716; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; HRFLYAE; -.
DR Proteomes; UP000001010; 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 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; Reference proteome.
FT CHAIN 1..323
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095431"
FT DOMAIN 21..106
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 127..317
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 167
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 191
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 269
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 272
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 295
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 304
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ SEQUENCE 323 AA; 36049 MW; 2CD56DE56EDFC3B4 CRC64;
MSASSPAERR QRAQQLPPLR AEDDQAIQRF LDRLWAEQGV ARQTLDSYRR DLEGLARWRD
GAGGGLQGAD RSALFDYLRW RTEARYAPRS NARLLSTLRG FYALCLRDGV RSDDPTALLD
PPRLPRSLPK ALTESQIDAL LAAPEIGTPL GLRDRAMLEL MYAAGLRVSE LVTLPAVAIN
LRQGVLRVTG KGSKERLVPL GEESQHWLER YLETARPTLS ERKAVPAVDG QVPLFIDAAR
RPLSRQQFWG LVKRYAAVAG IDPDTVSPHG LRHSFATHLL NHGADLRALQ MLLGHSSLST
TQIYTLVARQ HLQTLHARHH PRG
