XERC_RALPJ
ID XERC_RALPJ Reviewed; 328 AA.
AC B2U7W2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=Rpic_3697;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001068; ACD28815.1; -; Genomic_DNA.
DR RefSeq; WP_004628279.1; NC_010682.1.
DR AlphaFoldDB; B2U7W2; -.
DR SMR; B2U7W2; -.
DR STRING; 402626.Rpic_3697; -.
DR EnsemblBacteria; ACD28815; ACD28815; Rpic_3697.
DR KEGG; rpi:Rpic_3697; -.
DR eggNOG; COG4973; Bacteria.
DR HOGENOM; CLU_027562_9_0_4; -.
DR OMA; HSFASHM; -.
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 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; IPR011931; Recomb_XerC.
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; TIGR02224; recomb_XerC; 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..328
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000187611"
FT DOMAIN 13..100
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 122..319
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 197
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 271
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 274
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 297
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 306
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 328 AA; 36119 MW; 329171134BE864F3 CRC64;
MPQSASVDDH GAQAPHPQIA AYLDALKFER QLSPHTLQSY TRELAVLQRL GAQHAANIDL
TQLQSHHIRR MMAQLHGDGL SGRSIARALS AWRGWFKWMA LRDAAVTANP VDGVRAPKSP
KRLPKALSVE QAVALMEQLP GDDAETIRDR AVNELFYSCG LRLSELVSLD MRHVKAGAYE
SASWLDLEAR EVQVLGKGSK RRTVPVGTKA TEALAAWLAV RAQLAKSDAA PEDAHALFLS
PRGKRLAQRQ IQLRMKRNAI AAGVPADVHP HVLRHSFATH MLQSSGDLRA VQELLGHASI
ASTQVYTSLD FQHLAKIYDQ AHPRAKKK