XERC_BIFLS
ID XERC_BIFLS Reviewed; 355 AA.
AC B7GQE1; E8MRA3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN OrderedLocusNames=Blon_0921, BLIJ_0938;
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
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; CP001095; ACJ52021.1; -; Genomic_DNA.
DR EMBL; AP010889; BAJ68528.1; -; Genomic_DNA.
DR RefSeq; WP_012577287.1; NZ_JDTT01000006.1.
DR AlphaFoldDB; B7GQE1; -.
DR SMR; B7GQE1; -.
DR PRIDE; B7GQE1; -.
DR EnsemblBacteria; ACJ52021; ACJ52021; Blon_0921.
DR KEGG; bln:Blon_0921; -.
DR KEGG; blon:BLIJ_0938; -.
DR PATRIC; fig|391904.8.peg.948; -.
DR HOGENOM; CLU_027562_9_0_11; -.
DR OMA; QAFWYLI; -.
DR Proteomes; UP000001360; 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_1000187583"
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 138..180
FT /note="Disordered"
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; 38404 MW; 444976A6C3D462DC CRC64;
MSSTQFDGDI DSFVSYLKSN RGLSANTLKA YRADLTACLH LFELRGVTDL NEITLDDLRS
WMAVESRDHA RSSMARKTVA VRGFFAWAYE HGLTATDPAA TLMTPSIPST LPAVLTESQA
EQLLDVAEHA VATNQYKDDG GAAAASGSGK AAGKTADKSA DTVNRSEAPA RADKRDNARV
TAESQRNAAI LELLYATGIR VAELVSMDIA DIDFSNRTIK VTGKGNKQRV VPFGLPAQRA
LETWLEQGRP VLARTATDAV KSRAANALFL GARGGRIDQR IARDIVHRAA REAGVPDISP
HALRHSAATH ILDGGADLRE VQEMLGHSSL KTTQRYTHVS IEQLKNRYGQ AFPRA
