XERD_MYCLE
ID XERD_MYCLE Reviewed; 316 AA.
AC Q49890; O05671;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; OrderedLocusNames=ML1365;
GN ORFNames=MLC1351.07c, u0247d;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U00021; AAA50925.1; -; Genomic_DNA.
DR EMBL; Z95117; CAB08282.1; -; Genomic_DNA.
DR EMBL; AL583921; CAC31746.1; -; Genomic_DNA.
DR PIR; G87079; G87079.
DR PIR; S72959; S72959.
DR RefSeq; NP_301974.1; NC_002677.1.
DR RefSeq; WP_010908295.1; NC_002677.1.
DR AlphaFoldDB; Q49890; -.
DR SMR; Q49890; -.
DR STRING; 272631.ML1365; -.
DR PRIDE; Q49890; -.
DR EnsemblBacteria; CAC31746; CAC31746; CAC31746.
DR KEGG; mle:ML1365; -.
DR PATRIC; fig|272631.5.peg.2523; -.
DR Leproma; ML1365; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_11; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000000806; 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 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..316
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095397"
FT DOMAIN 4..97
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 118..309
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 186
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 261
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 296
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT CONFLICT 140
FT /note="R -> G (in Ref. 1; AAA50925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 33975 MW; B77113701BFD6A26 CRC64;
MTTAALQTQL QGYLDYLIIE RSIAANTLSS YRRDLIRYSK HLSDRGIEDL AKVGEHDVSE
FLVALRRGDP DSGVAALSAV SAARALIAVR GLHRFAVAEG LVDLDVARAV RPPTPGRRLP
KSLTVDEVLA LLESVGGESR ADGPLVLRNR ALLELLYSTG SRISEAVGLD VDDVDTQART
VLLQGKGGKQ RLVPVGRPAV QALDAYLVRG RSDLARRGPG MLATPAIFLN ARGGRLSRQS
AWQVLQDAAE HAGITSGVSP HMLRHSFATH LLEGGADIRV VQELMGHASV TTTQIYTLVT
VQALREVWAG AHPRAK
