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XERS_STRR6
ID   XERS_STRR6              Reviewed;         356 AA.
AC   Q7ZAK7;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=spr1046;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   FUNCTION AS A RECOMBINASE, AND ACTIVITY REGULATION.
RC   STRAIN=ATCC BAA-255 / R6;
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.
RX   PubMed=25569614; DOI=10.1371/journal.pgen.1004934;
RA   Johnston C., Mortier-Barriere I., Granadel C., Polard P., Martin B.,
RA   Claverys J.P.;
RT   "RecFOR is not required for pneumococcal transformation but together with
RT   XerS for resolution of chromosome dimers frequently formed in the
RT   process.";
RL   PLoS Genet. 11:E1004934-E1004934(2015).
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). Required for
CC       resolution of chromosome dimers frequently formed by transformation
CC       (PubMed:25569614). {ECO:0000269|PubMed:17630835,
CC       ECO:0000269|PubMed:25569614}.
CC   -!- ACTIVITY REGULATION: FtsK is required for recombination.
CC       {ECO:0000255|HAMAP-Rule:MF_01816, ECO:0000269|PubMed:17630835}.
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; AE007317; AAK99850.1; -; Genomic_DNA.
DR   PIR; F98002; F98002.
DR   RefSeq; NP_358640.1; NC_003098.1.
DR   RefSeq; WP_000817882.1; NC_003098.1.
DR   AlphaFoldDB; Q7ZAK7; -.
DR   SMR; Q7ZAK7; -.
DR   STRING; 171101.spr1046; -.
DR   EnsemblBacteria; AAK99850; AAK99850; spr1046.
DR   GeneID; 60233685; -.
DR   GeneID; 66806283; -.
DR   KEGG; spr:spr1046; -.
DR   PATRIC; fig|171101.6.peg.1137; -.
DR   eggNOG; COG4974; Bacteria.
DR   HOGENOM; CLU_027562_9_6_9; -.
DR   OMA; EKNGAHM; -.
DR   Proteomes; UP000000586; 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: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; PF02899; Phage_int_SAM_1; 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; Reference proteome.
FT   CHAIN           1..356
FT                   /note="Tyrosine recombinase XerS"
FT                   /id="PRO_0000095364"
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"
SQ   SEQUENCE   356 AA;  41171 MW;  1E3C68618B650155 CRC64;
     MKREILLERI DKLKQLMPWY VLEYYQSKLA VPYSFTTLYE YLKEYDRFFS WVLESGISNA
     DKISDIPLSV LENMSKKDME SFILYLRERP LLNANTTKQG VSQTTINRTL SALSSLYKYL
     TEEVENDQGE PYFYRNVMKK VSTKKKKETL AARAENIKQK LFLGDETEGF LTYIDQEHPQ
     QLSNRALSSF NKNKERDLAI IALLLASGVR LSEAVNLDLR DLNLKMMVID VTRKGGKRDS
     VNVAAFAKPY LENYLAIRNQ RYKTEKTDTA LFLTLYRGVP NRIDASSVEK MVAKYSEDFK
     VRVTPHKLRH TLATRLYDAT KSQVLVSHQL GHASTQVTDL YTHIVNDEQK NALDSL
 
 
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