XERC_ECO57
ID XERC_ECO57 Reviewed; 298 AA.
AC Q8X4T6;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN OrderedLocusNames=Z5328, ECs4741;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG59004.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38164.1; -; Genomic_DNA.
DR PIR; E91221; E91221.
DR PIR; H86067; H86067.
DR RefSeq; NP_312768.1; NC_002695.1.
DR RefSeq; WP_000130682.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X4T6; -.
DR SMR; Q8X4T6; -.
DR STRING; 155864.EDL933_5130; -.
DR EnsemblBacteria; AAG59004; AAG59004; Z5328.
DR EnsemblBacteria; BAB38164; BAB38164; ECs_4741.
DR GeneID; 912638; -.
DR KEGG; ece:Z5328; -.
DR KEGG; ecs:ECs_4741; -.
DR PATRIC; fig|386585.9.peg.4948; -.
DR eggNOG; COG4973; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome.
FT CHAIN 1..298
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_0000095296"
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; 33879 MW; 9C420BBAA7D837D0 CRC64;
MTDLHTDVER YLRYLSVERQ LSPITLLNYQ RQLEAIINFA SENGLQNWQQ CDAAMVRNFA
VRSRRKGLGA ASLALRLSAL RSFFDWLVSQ NELKANPAKG VSAPKTPRHL PKNIDVDDIN
RLLDIDINDP LAVRDRAMLE VMYGAGLRLS ELVGLDIKHL DLESGEVWVM GKGSKERRLP
IGRNALSWIE HWLDLRDLFG SEDDALFLSK LGKRISARNV QKRFAEWGIK QGLNNHVHPH
KLRHSFATHM LESSGDLRGV QELLGHANLS TTQIYTHLDF QHLASVYDAA HPRAKRGK
