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XERS_LACLM
ID   XERS_LACLM              Reviewed;         356 AA.
AC   A2RKP9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Tyrosine recombinase XerS {ECO:0000255|HAMAP-Rule:MF_01816, ECO:0000305};
GN   Name=xerS {ECO:0000255|HAMAP-Rule:MF_01816, ECO:0000303|PubMed:17630835};
GN   OrderedLocusNames=llmg_1270;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [2]
RP   FUNCTION AS A RECOMBINASE.
RC   STRAIN=MG1363;
RX   PubMed=17630835; DOI=10.1371/journal.pgen.0030117;
RA   Le Bourgeois P., Bugarel M., Campo N., Daveran-Mingot M.-L., Labonte J.,
RA   Lanfranchi D., Lautier T., Pages C., Ritzenthaler P.;
RT   "The unconventional Xer recombination machinery of
RT   Streptococci/Lactococci.";
RL   PLoS Genet. 3:E117-E117(2007).
RN   [3]
RP   FUNCTION AS A RECOMBINASE, DNA-BINDING, ACTIVITY REGULATION, AND
RP   MUTAGENESIS OF TYR-341.
RX   PubMed=20542912; DOI=10.1093/nar/gkq507;
RA   Nolivos S., Pages C., Rousseau P., Le Bourgeois P., Cornet F.;
RT   "Are two better than one? Analysis of an FtsK/Xer recombination system that
RT   uses a single recombinase.";
RL   Nucleic Acids Res. 38:6477-6489(2010).
CC   -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC       the cutting and rejoining of the recombining DNA molecules. Essential
CC       to convert dimers of the bacterial chromosome into monomers to permit
CC       their segregation at cell division (PubMed:17630835, PubMed:20542912).
CC       Binds an atypical recombination dif site (difSL). Binds preferentially
CC       to the left arm and cooperatively to the right arm of difSL
CC       (PubMed:20542912). {ECO:0000269|PubMed:17630835,
CC       ECO:0000269|PubMed:20542912}.
CC   -!- ACTIVITY REGULATION: FtsK is required for recombination.
CC       {ECO:0000255|HAMAP-Rule:MF_01816, ECO:0000269|PubMed:20542912}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01816,
CC       ECO:0000305}.
CC   -!- MISCELLANEOUS: In contrast to the XerC-XerD complex present in non-
CC       streptococcaceae bacteria, XerS acts as a single recombinase required
CC       to recombine difSL recombination site. {ECO:0000305|PubMed:17630835}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerS subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01816, ECO:0000305}.
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DR   EMBL; AM406671; CAL97863.1; -; Genomic_DNA.
DR   RefSeq; WP_011835149.1; NZ_WJVF01000013.1.
DR   AlphaFoldDB; A2RKP9; -.
DR   SMR; A2RKP9; -.
DR   STRING; 416870.llmg_1270; -.
DR   EnsemblBacteria; CAL97863; CAL97863; llmg_1270.
DR   GeneID; 61109491; -.
DR   KEGG; llm:llmg_1270; -.
DR   eggNOG; COG4974; Bacteria.
DR   HOGENOM; CLU_027562_9_6_9; -.
DR   OMA; EKNGAHM; -.
DR   PhylomeDB; A2RKP9; -.
DR   BioCyc; LLAC416870:LLMG_RS06440-MON; -.
DR   Proteomes; UP000000364; 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; IMP:CACAO.
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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.150.130; -; 1.
DR   Gene3D; 1.10.443.10; -; 1.
DR   HAMAP; MF_01816; Recomb_XerS; 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; IPR023670; Recomb_XerS.
DR   Pfam; PF13495; Phage_int_SAM_4; 1.
DR   Pfam; PF00589; Phage_integrase; 1.
DR   SUPFAM; SSF56349; SSF56349; 1.
DR   PROSITE; PS51900; CB; 1.
DR   PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW   DNA integration; DNA recombination; DNA-binding.
FT   CHAIN           1..356
FT                   /note="Tyrosine recombinase XerS"
FT                   /id="PRO_0000372667"
FT   DOMAIN          16..121
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          169..354
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT                   Rule:MF_01816"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT                   Rule:MF_01816"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT                   Rule:MF_01816"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT                   Rule:MF_01816"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT                   Rule:MF_01816"
FT   ACT_SITE        341
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT                   Rule:MF_01816"
FT   MUTAGEN         341
FT                   /note="Y->F: Decrease in DNA binding. Lack of recombinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:20542912"
SQ   SEQUENCE   356 AA;  41307 MW;  A831073638B8B0EE CRC64;
     MKREQLIQNI EKLKHVMPPY VLEYYQSKLT IPYSLNTLYE YLKEYERFFS WLVDSGVADV
     DKITDVSLSV LENLTKRDLE SFILYLRERP RLNTHSTRYG VSQTTINRTL SALSSLYKYL
     TEEVENEDGE PYFYRNVMKK VQTKKKSETL ASRAENIKGK LFLGDETQGF LDYIDSEYEK
     TLSNRARSSF FKNKERDLAI IALILASGIR LSEAVNVDLR DLNLNTMIVE VTRKGGKRDA
     VPFAPFAKTY FERYLEVRSQ RYKTTAKDTA FFVTLYRDIA SRIDPSSVEK LVAKYSQAFK
     VRVTPHKLRH TLATRLYAQT NSQVLVSNQL GHASTQVTDL YTHIINEEQK NALDSL
 
 
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