XERD_LEPIN
ID XERD_LEPIN Reviewed; 298 AA.
AC Q7ZAM7;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; OrderedLocusNames=LA_2483;
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_01807}.
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_01807}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01807}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01807}.
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DR EMBL; AE010300; AAN49682.1; -; Genomic_DNA.
DR RefSeq; NP_712664.1; NC_004342.2.
DR RefSeq; WP_000204200.1; NC_004342.2.
DR AlphaFoldDB; Q7ZAM7; -.
DR SMR; Q7ZAM7; -.
DR STRING; 189518.LA_2483; -.
DR EnsemblBacteria; AAN49682; AAN49682; LA_2483.
DR GeneID; 61144777; -.
DR KEGG; lil:LA_2483; -.
DR PATRIC; fig|189518.3.peg.2462; -.
DR HOGENOM; CLU_027562_9_6_12; -.
DR InParanoid; Q7ZAM7; -.
DR OMA; QAFWYLI; -.
DR PRO; PR:Q7ZAM7; -.
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 HAMAP; MF_01807; Recomb_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; IPR011932; Recomb_XerD.
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; TIGR02225; recomb_XerD; 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..298
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095393"
FT DOMAIN 3..88
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 109..292
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 173
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 247
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 270
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 279
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ SEQUENCE 298 AA; 35073 MW; F1578AA6F23FEB25 CRC64;
MTSSHNNLLQ NFQEYLSVEK GLSDNSIYSY GYDLNKFKNF LEKEHIDFLK VQADDIMRFL
NEEKDRKISS KTIAREVVAI RQFYKFLKDE KKLDTNPTEK IETPEVMRSI PDYLTQDEIE
ELFASIKEDN LYELRDKCIF ELLYSSGLRI SEACNLRLND MDLEGMTLTV EGKGGRQRLV
PFGEKSLDIL NRYLKQSRPF ILKSRNCEYL FVSKKGSYIN RKSVWRLLNH YIKRTSILKK
VTPHTLRHSF ATHLLENHAD LKSVQELLGH IDIATTQIYT HMANKTLREV HKKFHPRG
