XERD_RICBR
ID XERD_RICBR Reviewed; 305 AA.
AC Q1RHT1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; OrderedLocusNames=RBE_1002;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05083.1; -; Genomic_DNA.
DR RefSeq; WP_011477663.1; NC_007940.1.
DR AlphaFoldDB; Q1RHT1; -.
DR SMR; Q1RHT1; -.
DR STRING; 336407.RBE_1002; -.
DR EnsemblBacteria; ABE05083; ABE05083; RBE_1002.
DR KEGG; rbe:RBE_1002; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_5; -.
DR OMA; QAFWYLI; -.
DR OrthoDB; 745068at2; -.
DR Proteomes; UP000001951; 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 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..305
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000272368"
FT DOMAIN 1..83
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 104..298
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 145
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 253
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 285
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ SEQUENCE 305 AA; 34689 MW; B98383395AFBC544 CRC64;
MEFISQFLEM LLAERALSKN SILSYKRDLL DFHNYLAKQK LSELNITTDN IRNWVEYLAE
NSLQARSINR KISTIKSYYE FLISENHTNL NPLLNIDLPK YQNKLPEILS IDDIKSLLEY
CSQDISPEGA RLNAMIHLLY ASGLRVSELV SLKLSDILSN KVSREVKKIF SVLGKGNKER
IIVINEPAIN SLVKYLVVRD NFVNKTKPKN LIYLFPSSAA AGYMTRQNFA ILLKSAALYA
GLNPEHISPH VLRHSFASHL LEGGADLRVI QELLGHADIS TTQIYTHLQT NHLKKALLHH
PLSKN