GenomeNet

Database: UniProt
Entry: A0A099W7A9_9LIST
LinkDB: A0A099W7A9_9LIST
Original site: A0A099W7A9_9LIST 
ID   A0A099W7A9_9LIST        Unreviewed;       297 AA.
AC   A0A099W7A9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Tyrosine recombinase XerD {ECO:0000256|ARBA:ARBA00015810, ECO:0000256|HAMAP-Rule:MF_01807};
GN   Name=xerD {ECO:0000256|HAMAP-Rule:MF_01807};
GN   ORFNames=EP57_08880 {ECO:0000313|EMBL:KGL40661.1};
OS   Listeria booriae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL40661.1, ECO:0000313|Proteomes:UP000029844};
RN   [1] {ECO:0000313|EMBL:KGL40661.1, ECO:0000313|Proteomes:UP000029844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL40661.1,
RC   ECO:0000313|Proteomes:UP000029844};
RA   den Bakker H.C.;
RT   "Novel Listeriaceae from food processing environments.";
RL   Submitted (MAY-2014) 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:0000256|HAMAP-Rule:MF_01807}.
CC   -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC       molecules of XerC and two molecules of XerD. {ECO:0000256|HAMAP-
CC       Rule:MF_01807}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01807}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.
CC       {ECO:0000256|ARBA:ARBA00010450, ECO:0000256|HAMAP-Rule:MF_01807}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGL40661.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JNFA01000023; KGL40661.1; -; Genomic_DNA.
DR   RefSeq; WP_036085870.1; NZ_UGPF01000002.1.
DR   AlphaFoldDB; A0A099W7A9; -.
DR   STRING; 1552123.EP57_08880; -.
DR   GeneID; 58717487; -.
DR   eggNOG; COG4974; Bacteria.
DR   OrthoDB; 9801717at2; -.
DR   Proteomes; UP000029844; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-UniRule.
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:DNA transposition; IEA:UniProtKB-UniRule.
DR   CDD; cd00798; INT_XerDC_C; 1.
DR   Gene3D; 1.10.150.130; -; 1.
DR   Gene3D; 1.10.443.10; Intergrase catalytic core; 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   NCBIfam; TIGR02225; recomb_XerD; 1.
DR   PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR   PANTHER; PTHR30349:SF87; PROPHAGE INTEGRASE INTD-RELATED; 1.
DR   Pfam; PF02899; Phage_int_SAM_1; 1.
DR   Pfam; PF00589; Phage_integrase; 1.
DR   SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR   PROSITE; PS51900; CB; 1.
DR   PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01807};
KW   DNA integration {ECO:0000256|ARBA:ARBA00022908, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01807}; Reference proteome {ECO:0000313|Proteomes:UP000029844}.
FT   DOMAIN          1..86
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          107..291
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        278
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
SQ   SEQUENCE   297 AA;  34085 MW;  EBE73F3B75A76AAB CRC64;
     MNDLILDFLH FLQVEKGLAT NTLTAYERDL RYFARYLEEE QGGMAIRDVE RIHIVGFMAF
     AKSEGKSPRT VARYIASLRS FFHFLLHEKL ADRDPMIQIE TPKQAQGLPK ILNLNDVEKL
     LETPDGAKPL GMRDKAMLEV LYATGLRVTE LVNLQMDDLH LQMGFIQTIG KGDKERIIPL
     GKKATTVLER YLEFGRPRLR RASERNDFVF LNHHGRGMTR QGFWKNLKQI AAKAGIDKPI
     TPHTLRHSFA THLLENGADL RSVQELLGHA DISTTQIYTH VTKARLKDVY KQYHPRA
//
DBGET integrated database retrieval system