XERC_RICBR
ID XERC_RICBR Reviewed; 305 AA.
AC Q1RK56;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=RBE_0177;
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_01808}.
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_01808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01808}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01808}.
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DR EMBL; CP000087; ABE04258.1; -; Genomic_DNA.
DR RefSeq; WP_011476872.1; NC_007940.1.
DR AlphaFoldDB; Q1RK56; -.
DR SMR; Q1RK56; -.
DR STRING; 336407.RBE_0177; -.
DR EnsemblBacteria; ABE04258; ABE04258; RBE_0177.
DR KEGG; rbe:RBE_0177; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_5; -.
DR OMA; TKVTVEH; -.
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 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; 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 XerC"
FT /id="PRO_0000272365"
FT DOMAIN 4..95
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 116..298
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 159
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 182
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 253
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 285
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 305 AA; 35517 MW; 90B2290F98289409 CRC64;
MLDTQIQELI IKWQKYLSLQ KNYSNHTLIS YNNDLKHFLE FMNYYNSDIV TMDYIKAADI
RLMRSWLAKR KCDNFVTSSI ARGLSAIKNF YKFLEKTAEL HNHVVFSIKS PKKSKLLPKA
LSEEEVNISL DHIEEYGNSQ WIEIRNKALL VLIYASGLRI SEALSITKLH LQNLEFIKIM
GKGSKERVIP WLAIARNLIT EYLEKLPYEL KDDEPIFRGK QGKKLQPPVF NRELIKLKRF
YGLPEYLSAH SFRHSFASHL LENGADLRSI QELLGHKSLS TTQSYTKTSI KHLETAYVTA
HPIKK