ID   XERD_LACCA              Reviewed;         293 AA.
AC   Q93C64;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN   Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807};
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Flandin J.-F., Teijeiro S., Szatmari G.B.;
RT   "The cloning and characterization of the Lactobacillus casei xerD gene.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
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; AF413208; AAL07436.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93C64; -.
DR   SMR; Q93C64; -.
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.
FT   CHAIN           1..293
FT                   /note="Tyrosine recombinase XerD"
FT                   /id="PRO_0000095391"
FT   DOMAIN          1..83
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          104..287
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        274
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ   SEQUENCE   293 AA;  33230 MW;  CD85C8CC247ACA9F CRC64;
     MHGLIADFIH YLDVERGLAR TTQVSYQQDL TTFMAWLSDQ KQTTFPEDFG VIQAFLKHQN
     DTKAPASVSR MISALRKFYR FLLREGAIKS DPMTKIDTPK KAQHLPATLS GTEIDALMAK
     PDTTKPLGLR DRAIFELMYA TGLRVSEVVG LRLDQLHLAM NLLQVTGKGD KERLVPISPQ
     AADWVNRYLQ ESRPRLIKHQ QPKAVFVNFH GHALTRQVIW KNLKAYIASV GIEKDVTPHT
     LRHSFATRLL ENGADLRVVQ ELLGHSDIST TQIYTHLSNQ HLVAVYHKTH PRG