XERC_ECOLI
ID XERC_ECOLI Reviewed; 298 AA.
AC P0A8P6; P22885; Q2M8B7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Tyrosine recombinase XerC;
GN Name=xerC; OrderedLocusNames=b3811, JW3784;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=2254268; DOI=10.1128/jb.172.12.6973-6980.1990;
RA Colloms S.D., Sykora P., Szatmari G., Sherratt D.J.;
RT "Recombination at ColE1 cer requires the Escherichia coli xerC gene
RT product, a member of the lambda integrase family of site-specific
RT recombinases.";
RL J. Bacteriol. 172:6973-6980(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 184-185.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION, AND MUTAGENESIS OF TYR-275.
RC STRAIN=K12 / DS941;
RX PubMed=8402918; DOI=10.1016/0092-8674(93)80076-q;
RA Blakely G., May G., McCulloch R., Arciszewska L.K., Burke M., Lovett S.T.,
RA Sherratt D.J.;
RT "Two related recombinases are required for site-specific recombination at
RT dif and cer in E. coli K12.";
RL Cell 75:351-361(1993).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ARG-243 AND TYR-275.
RC STRAIN=K12 / DS941;
RX PubMed=7744017; DOI=10.1002/j.1460-2075.1995.tb07203.x;
RA Arciszewska L.K., Sherratt D.J.;
RT "Xer site-specific recombination in vitro.";
RL EMBO J. 14:2112-2120(1995).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF TYR-275.
RX PubMed=9268326; DOI=10.1074/jbc.272.35.21927;
RA Cornet F., Hallet B., Sherratt D.J.;
RT "Xer recombination in Escherichia coli. Site-specific DNA topoisomerase
RT activity of the XerC and XerD recombinases.";
RL J. Biol. Chem. 272:21927-21931(1997).
RN [8]
RP INTERACTION WITH XERC.
RC STRAIN=K12 / DS941;
RX PubMed=10361305; DOI=10.1046/j.1365-2958.1999.01418.x;
RA Spiers A.J., Sherratt D.J.;
RT "C-terminal interactions between the XerC and XerD site-specific
RT recombinases.";
RL Mol. Microbiol. 32:1031-1042(1999).
RN [9]
RP FUNCTION.
RX PubMed=10037776; DOI=10.1074/jbc.274.10.6763;
RA Grainge I., Sherratt D.J.;
RT "Xer site-specific recombination. DNA strand rejoining by recombinase
RT XerC.";
RL J. Biol. Chem. 274:6763-6769(1999).
RN [10]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF 252-GLU--SER-254.
RC STRAIN=K12 / DS941;
RX PubMed=10635320; DOI=10.1016/s1097-2765(00)80224-5;
RA Hallet B., Arciszewska L.K., Sherratt D.J.;
RT "Reciprocal control of catalysis by the tyrosine recombinases XerC and
RT XerD: an enzymatic switch in site-specific recombination.";
RL Mol. Cell 4:949-959(1999).
RN [11]
RP ACTIVITY REGULATION BY FTSK.
RX PubMed=11832210; DOI=10.1016/s0092-8674(02)00624-4;
RA Aussel L., Barre F.-X., Aroyo M., Stasiak A., Stasiak A.Z., Sherratt D.J.;
RT "FtsK is a DNA motor protein that activates chromosome dimer resolution by
RT switching the catalytic state of the XerC and XerD recombinases.";
RL Cell 108:195-205(2002).
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 at ColE1 xer (or
CC cer) and pSC101 (or psi) sites. In the complex XerC specifically
CC exchanges the top DNA strands (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10037776, ECO:0000269|PubMed:7744017,
CC ECO:0000269|PubMed:9268326}.
CC -!- ACTIVITY REGULATION: During recombination, the heterotetrameric complex
CC catalyzes two consecutive pairs of strand exchanges, implying that
CC specific pairs of active sites are sequentially switched on and off in
CC the recombinase tetramer to ensure that appropriate DNA strands will be
CC exchanged at both reaction steps. FtsK plays a central role in this
CC catalytic state switch that turns recombinase on and off reciprocally.
CC The reciprocal C-terminal interaction between XerC and XerD may also
CC participate in the enzymatic switch process.
CC {ECO:0000269|PubMed:10635320, ECO:0000269|PubMed:11832210}.
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:0000269|PubMed:10361305}.
CC -!- INTERACTION:
CC P0A8P6; P0A9E0: araC; NbExp=3; IntAct=EBI-1133806, EBI-1113479;
CC P0A8P6; P77551: rzpR; NbExp=2; IntAct=EBI-1133806, EBI-9135212;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with DNA.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000305}.
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DR EMBL; M38257; AAA24763.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67607.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76814.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77489.1; -; Genomic_DNA.
DR PIR; C37841; C37841.
DR RefSeq; NP_418256.1; NC_000913.3.
DR RefSeq; WP_000130691.1; NZ_SSZK01000025.1.
DR PDB; 5DCF; X-ray; 2.30 A; A=111-298.
DR PDBsum; 5DCF; -.
DR AlphaFoldDB; P0A8P6; -.
DR SMR; P0A8P6; -.
DR BioGRID; 4263112; 411.
DR BioGRID; 852652; 6.
DR ComplexPortal; CPX-5123; XerCD site-specific tyrosine recombinase complex.
DR DIP; DIP-726N; -.
DR IntAct; P0A8P6; 9.
DR STRING; 511145.b3811; -.
DR jPOST; P0A8P6; -.
DR PaxDb; P0A8P6; -.
DR PRIDE; P0A8P6; -.
DR EnsemblBacteria; AAC76814; AAC76814; b3811.
DR EnsemblBacteria; BAE77489; BAE77489; BAE77489.
DR GeneID; 66672282; -.
DR GeneID; 948355; -.
DR KEGG; ecj:JW3784; -.
DR KEGG; eco:b3811; -.
DR PATRIC; fig|1411691.4.peg.2896; -.
DR EchoBASE; EB1062; -.
DR eggNOG; COG4973; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR InParanoid; P0A8P6; -.
DR OMA; HSFASHM; -.
DR PhylomeDB; P0A8P6; -.
DR BioCyc; EcoCyc:EG11069-MON; -.
DR PRO; PR:P0A8P6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IDA:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0009009; F:site-specific recombinase activity; IDA:EcoliWiki.
DR GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IDA:EcoliWiki.
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; IDA:ComplexPortal.
DR GO; GO:0006276; P:plasmid maintenance; IMP:EcoliWiki.
DR GO; GO:0042150; P:plasmid recombination; IMP:EcoliWiki.
DR GO; GO:0071139; P:resolution of recombination intermediates; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW Direct protein sequencing; DNA integration; DNA recombination; DNA-binding;
KW Reference proteome.
FT CHAIN 1..298
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_0000095294"
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|PROSITE-ProRule:PRU01246"
FT ACT_SITE 172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 275
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT MUTAGEN 243
FT /note="R->Q: Abolishes DNA cleavage activity."
FT /evidence="ECO:0000269|PubMed:7744017"
FT MUTAGEN 252..254
FT /note="ESS->NHG: Abolishes chromosomal recombination but
FT not plasmid resolution."
FT /evidence="ECO:0000269|PubMed:10635320"
FT MUTAGEN 275
FT /note="Y->F: Abolishes DNA cleavage activity."
FT /evidence="ECO:0000269|PubMed:7744017,
FT ECO:0000269|PubMed:8402918, ECO:0000269|PubMed:9268326"
FT CONFLICT 184..185
FT /note="NA -> KP (in Ref. 2; AAA67607)"
FT /evidence="ECO:0000305"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:5DCF"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:5DCF"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5DCF"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:5DCF"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:5DCF"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:5DCF"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:5DCF"
SQ SEQUENCE 298 AA; 33868 MW; 91706E6945752FBA CRC64;
MTDLHTDVER YLRYLSVERQ LSPITLLNYQ RQLEAIINFA SENGLQSWQQ CDVTMVRNFA
VRSRRKGLGA ASLALRLSAL RSFFDWLVSQ NELKANPAKG VSAPKAPRHL PKNIDVDDMN
RLLDIDINDP LAVRDRAMLE VMYGAGLRLS ELVGLDIKHL DLESGEVWVM GKGSKERRLP
IGRNAVAWIE HWLDLRDLFG SEDDALFLSK LGKRISARNV QKRFAEWGIK QGLNNHVHPH
KLRHSFATHM LESSGDLRGV QELLGHANLS TTQIYTHLDF QHLASVYDAA HPRAKRGK
