XERC_LEPIN
ID XERC_LEPIN Reviewed; 311 AA.
AC Q7ZAM8;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=LA_2347;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC the cutting and rejoining of the recombining DNA molecules. The XerC-
CC XerD complex is essential to convert dimers of the bacterial chromosome
CC into monomers to permit their segregation at cell division. It also
CC contributes to the segregational stability of plasmids.
CC {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. {ECO:0000255|HAMAP-
CC 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; AE010300; AAN49546.2; -; Genomic_DNA.
DR RefSeq; NP_712528.2; NC_004342.2.
DR RefSeq; WP_002079116.1; NC_004342.2.
DR AlphaFoldDB; Q7ZAM8; -.
DR SMR; Q7ZAM8; -.
DR STRING; 189518.LA_2347; -.
DR PRIDE; Q7ZAM8; -.
DR EnsemblBacteria; AAN49546; AAN49546; LA_2347.
DR GeneID; 61144896; -.
DR KEGG; lil:LA_2347; -.
DR PATRIC; fig|189518.3.peg.2331; -.
DR HOGENOM; CLU_027562_9_2_12; -.
DR InParanoid; Q7ZAM8; -.
DR Proteomes; UP000001408; Chromosome I.
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..311
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_0000095301"
FT DOMAIN 14..100
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 121..303
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 187
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 255
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 258
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 281
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 290
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 311 AA; 36547 MW; B2C08DF4D19810E9 CRC64;
MGDYPFQFPE FSSESLNETA KKFINYLKIE KNYSQNTINA YSIDLKFFFE FCEKEQLDIF
QIEPVDIRSY FAYLAKKHEI DRRSQSRKLS SLRTFYKVLL REDLVKSNPA TQLSFPKVRK
EVPKNFRINE TEEILEFESE NASEVSEIRD RAMIEVLYSS GLRVFELVNA KLNSLSKDLT
VLKVLGKGRK ERFVYFGKEA VSSLQKYLEY RNVSFPDAEE IFLNQRGKKL TTRGVRYILN
ERRKKMGWEK TITPHKFRHT FATDLLDAGA EIRAVQELLG HSSLSTTQIY LSVSKEKIKE
VYRKAHPHAR K