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XERC_SALTY
ID   XERC_SALTY              Reviewed;         300 AA.
AC   P55888;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=STM3949;
GN   ORFNames=STMD1.41;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=9370270; DOI=10.1016/s0378-1119(97)00299-0;
RA   Hayes F., Lubetzki S.A., Sherratt D.J.;
RT   "Salmonella typhimurium specifies a circular chromosome dimer resolution
RT   system which is homologous to the Xer site-specific recombination system of
RT   Escherichia coli.";
RL   Gene 198:105-110(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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}.
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DR   EMBL; U92525; AAC45778.1; -; Genomic_DNA.
DR   EMBL; AF233324; AAF33443.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22793.1; -; Genomic_DNA.
DR   RefSeq; NP_462834.1; NC_003197.2.
DR   RefSeq; WP_000132874.1; NC_003197.2.
DR   AlphaFoldDB; P55888; -.
DR   SMR; P55888; -.
DR   STRING; 99287.STM3949; -.
DR   PaxDb; P55888; -.
DR   EnsemblBacteria; AAL22793; AAL22793; STM3949.
DR   GeneID; 1255475; -.
DR   KEGG; stm:STM3949; -.
DR   PATRIC; fig|99287.12.peg.4167; -.
DR   HOGENOM; CLU_027562_9_0_6; -.
DR   OMA; HSFASHM; -.
DR   PhylomeDB; P55888; -.
DR   BioCyc; SENT99287:STM3949-MON; -.
DR   Proteomes; UP000001014; 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..300
FT                   /note="Tyrosine recombinase XerC"
FT                   /id="PRO_0000095325"
FT   DOMAIN          4..90
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          111..290
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        277
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   300 AA;  33600 MW;  6BA0A0B39A2C9576 CRC64;
     MTDVALSQDV SRFLRYLGVE RQLSPITLLN YQRQLDAIIA LAGETGLKSW QQCDAAIVRS
     FAVRSRRKGL GPASLALRLS ALRSFFDWLV SQGELKANPA KGVSAPKAPR HLPKNIDVDD
     VNRLLDIDLN DPLAVRDRAM LEVMYGAGLR LSELVGLDIK HLDLDTGEVW VMGKGSKERR
     LPIGRNAVTW IEHWLDLRGL FASDEEALFL SKLGKRISAR NVQKRFAEWG IKQGLNSHVH
     PHKLRHSFAT HMLESSGDLR GVQELLGHAN LSTTQIYTHL DFQHLASVYD AAHPRAKRGK
 
 
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