XERC_ECOL5
ID XERC_ECOL5 Reviewed; 298 AA.
AC Q0TAR4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=ECP_4005;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC the cutting and rejoining of the recombining DNA molecules. Binds
CC cooperatively to specific DNA consensus sequences that are separated
CC from XerD binding sites by a short central region, forming the
CC heterotetrameric XerC-XerD complex that recombines DNA substrates. The
CC complex is essential to convert dimers of the bacterial chromosome into
CC monomers to permit their segregation at cell division. It also
CC contributes to the segregational stability of plasmids. In the complex
CC XerC specifically exchanges the top DNA strands. {ECO:0000255|HAMAP-
CC Rule:MF_01808}.
CC -!- ACTIVITY REGULATION: FtsK may regulate the catalytic switch between
CC XerC and XerD in the heterotetrameric complex during the two steps of
CC the recombination process. {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, in which XerC interacts
CC with XerD via its C-terminal region, XerD interacts with XerC via its
CC C-terminal region and so on. {ECO:0000255|HAMAP-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; CP000247; ABG71965.1; -; Genomic_DNA.
DR RefSeq; WP_000130675.1; NC_008253.1.
DR AlphaFoldDB; Q0TAR4; -.
DR SMR; Q0TAR4; -.
DR STRING; 362663.ECP_4005; -.
DR EnsemblBacteria; ABG71965; ABG71965; ECP_4005.
DR KEGG; ecp:ECP_4005; -.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000009182; 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; 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..298
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000070002"
FT DOMAIN 2..88
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 109..288
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 148
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 172
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 240
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 266
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 275
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 298 AA; 33834 MW; 6BCFDEFA07B5E012 CRC64;
MTDLHTDVER YLRYLSVERQ LSPITLLNYQ RQLEAIIHFA SENGLQSWQQ CDVTMVRNFA
VRSRRKGLGA AGLALRLSAL RSFFDWLVSQ NELKANPAKG VSAPKAPRHL PKNIDVDDMS
RLLDIDINDP LAVRDRAMLE VMYGAGLRLS ELVGLDIKHL DLESGEVWVM GKGSKERRLP
IGRNAVAWIE HWLDLRDLFG SEDDALFLSK LGKRISARNV QKRFAEWGIK QGLNNHVHPH
KLRHSFATHM LESSGDLRGV QELLGHANLS TTQIYTHLDF QHLASVYDAA HPRAKRGK