XERD_BRUAB
ID XERD_BRUAB Reviewed; 309 AA.
AC P0C122; Q57AM6; Q9FDG0;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Tyrosine recombinase XerD;
GN Name=xerD; OrderedLocusNames=BruAb1_2006;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX75308.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017223; AAX75308.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P0C122; -.
DR SMR; P0C122; -.
DR EnsemblBacteria; AAX75308; AAX75308; BruAb1_2006.
DR KEGG; bmb:BruAb1_2006; -.
DR HOGENOM; CLU_027562_9_0_5; -.
DR PRO; PR:P0C122; -.
DR Proteomes; UP000000540; Chromosome I.
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..309
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095374"
FT DOMAIN 3..88
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 109..302
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 289
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
SQ SEQUENCE 309 AA; 34130 MW; B24287E577CEDC33 CRC64;
MTMRASLAIE NFLEMMSAER GAAQNTLESY RRDLEAAAEE LAAKGVNLAE AETGHIRMTL
DTMAAQGFAP TSQARRLSAL RQFFRFLYSE GFRQDDPTGI LYAPKKQKPL PKIMSVENVG
KLLDRAALEA NEAAEPGERI KALRLHALLE TLYATGLRVS ELVGLPVTVA RTDHRFLLVR
GKGSKDRMVP LSRKARDALQ KFLTLRDSLP GSDDNPWLFP AFSESGHLAR QVFARELKGL
AARAGLAASS ASPHVLRHAF ASHLLQNGAD LRTVQQLLGH ADISTTQIYT HVLEERLHKL
VSEHHPLAD