XERD_PASMU
ID XERD_PASMU Reviewed; 297 AA.
AC Q9CPF0;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; OrderedLocusNames=PM0093;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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; AE004439; AAK02177.1; -; Genomic_DNA.
DR RefSeq; WP_010906477.1; NC_002663.1.
DR AlphaFoldDB; Q9CPF0; -.
DR SMR; Q9CPF0; -.
DR STRING; 747.DR93_1980; -.
DR EnsemblBacteria; AAK02177; AAK02177; PM0093.
DR KEGG; pmu:PM0093; -.
DR HOGENOM; CLU_027562_9_6_6; -.
DR OMA; QAFWYLI; -.
DR Proteomes; UP000000809; 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..297
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095403"
FT DOMAIN 1..86
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 107..291
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 171
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 269
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 278
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ SEQUENCE 297 AA; 34369 MW; 04B1F66CEE374964 CRC64;
MKDSALIELF LNEIWIEKQL SQNTIASYRL DLTALIQWLE KQQLTLINLD AIDLQTFLGE
RLNQGYKATS TARLLSAMRK LFQYLYREKY RTDDPSAVLS SPKLPSRLPK YLTEQQVTDL
LNSPDVDIPL ELRDKAMMEL LYATGLRVTE LVSLTIENIN INQGIVRVVG KGNKERIVPI
GEEATYWIRQ FMLYGRPFLL HGQSSDVVFP SKRALQMTRQ TFWHRIKHYA LLSDIDINSL
SPHVLRHAFA THLVNHGADL RVVQMLLGHS DLSTTQIYTH VAKERLKHLH ERYHPRG