ID   XERC_BIFLD              Reviewed;         355 AA.
AC   B3DQV1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=BLD_0251;
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=205913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A;
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
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; CP000605; ACD97697.1; -; Genomic_DNA.
DR   RefSeq; WP_008783120.1; NZ_AABM02000003.1.
DR   AlphaFoldDB; B3DQV1; -.
DR   SMR; B3DQV1; -.
DR   EnsemblBacteria; ACD97697; ACD97697; BLD_0251.
DR   GeneID; 66505454; -.
DR   KEGG; blj:BLD_0251; -.
DR   HOGENOM; CLU_027562_9_0_11; -.
DR   OMA; QAFWYLI; -.
DR   Proteomes; UP000002419; 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..355
FT                   /note="Tyrosine recombinase XerC"
FT                   /id="PRO_1000187582"
FT   DOMAIN          4..89
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          158..349
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   REGION          137..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        336
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   355 AA;  38462 MW;  8F78AA690F72AA46 CRC64;
     MSSTQFDGDI DSFVSYLKSN RGLSANTLKA YRADLTACLH LFELRGVTDL NEITLDDLRS
     WMAVESRDHA RSSMARKTVA VRGFFAWAYE HGLTTTDPAA TLMTPSIPST LPAVLTESQA
     EQLLDVAEHA VATNQYKDDG GAAAAPGSGK AAGKTADKSA DTVNRSEAPA RADKRDNARV
     TAESQRNAAI LELLYATGIR VAELVSMDIA DIDFSNRTIK VTGKGNKQRV VPFGLPAQRA
     LETWLEQGRP VLARTATDAV KSRAANALFL GARGGRIDQR IARDIVHRAA REAGVPDISP
     HALRHSAATH MLDGGADLRE VQEMLGHSSL KTTQRYTHVS IEQLKNRYGQ AFPRA