XERD_PROMI
ID XERD_PROMI Reviewed; 313 AA.
AC O31206;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807};
OS Proteus mirabilis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DNA-BINDING.
RC STRAIN=UM-240-82;
RX PubMed=9675854; DOI=10.1111/j.1574-6968.1998.tb13071.x;
RA Villion M., Szatmari G.;
RT "Cloning and characterisation of the Proteus mirabilis xerD gene.";
RL FEMS Microbiol. Lett. 164:83-90(1998).
CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC the cutting and rejoining of the recombining DNA molecules. Binds
CC cooperatively to specific DNA consensus sequences that are separated
CC from XerC binding sites by a short central region, forming the
CC heterotetrameric XerC-XerD complex that recombines DNA substrates. The
CC complex is essential to convert dimers of the bacterial chromosome into
CC monomers to permit their segregation at cell division. It also
CC contributes to the segregational stability of plasmids. In the complex
CC XerD specifically exchanges the bottom DNA strands. {ECO:0000255|HAMAP-
CC Rule:MF_01807}.
CC -!- ACTIVITY REGULATION: FtsK may regulate the catalytic switch between
CC XerC and XerD in the heterotetrameric complex during the two steps of
CC the recombination process. {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, in which XerC interacts
CC with XerD via its C-terminal region, XerD interacts with XerC via its
CC C-terminal region and so on. {ECO:0000255|HAMAP-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; AF033497; AAB87499.1; -; Genomic_DNA.
DR RefSeq; WP_004244032.1; NZ_WURR01000002.1.
DR AlphaFoldDB; O31206; -.
DR SMR; O31206; -.
DR STRING; 584.AOUC001_04720; -.
DR PRIDE; O31206; -.
DR GeneID; 6803432; -.
DR PATRIC; fig|584.106.peg.2483; -.
DR OMA; QAFWYLI; -.
DR OrthoDB; 745068at2; -.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA integration; DNA recombination; DNA-binding.
FT CHAIN 1..313
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095404"
FT DOMAIN 17..102
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 123..307
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 187
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 259
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 262
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 294
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ SEQUENCE 313 AA; 35760 MW; 864FF792DE078758 CRC64;
MTQTKLSTQT TTDNNQEDND VIIEQFLDSI WLEQGLSANT LSAYRLDLQA LSQWLVTQKL
NWLSVTTLDL HAFLATRLDE GYKATSAARL LSTLRRFFQY LYREKLRQDD PSALLSTPKL
PKRLPKDLSE QQVENLLSAP CIDEPIELRD KAMLEVLYAC GLRVSELVGL SLSDISLRQG
VLRVIGKGDK ERLVPLGEEA IYWLEQYLQY GRPALMQGKT DDIVFPSLRG QKMTRQTFWH
RIKHYAVIAG IDSEKLSPHV LRHAFATHLL NHGADLRVVQ MLLGHSDLST TQIYTHVATE
RLKVLHQQHH PRG