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Database: UniProt
Entry: A0A0R1N1I0_9LACO
LinkDB: A0A0R1N1I0_9LACO
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ID   A0A0R1N1I0_9LACO        Unreviewed;       296 AA.
AC   A0A0R1N1I0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=FD09_GL001304 {ECO:0000313|EMBL:KRL14143.1};
OS   Schleiferilactobacillus perolens DSM 12744.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Schleiferilactobacillus.
OX   NCBI_TaxID=1423792 {ECO:0000313|EMBL:KRL14143.1, ECO:0000313|Proteomes:UP000051330};
RN   [1] {ECO:0000313|EMBL:KRL14143.1, ECO:0000313|Proteomes:UP000051330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12744 {ECO:0000313|EMBL:KRL14143.1,
RC   ECO:0000313|Proteomes:UP000051330};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRL14143.1}.
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DR   EMBL; AZEC01000002; KRL14143.1; -; Genomic_DNA.
DR   RefSeq; WP_057818082.1; NZ_AZEC01000002.1.
DR   AlphaFoldDB; A0A0R1N1I0; -.
DR   STRING; 1423792.FD09_GL001304; -.
DR   PATRIC; fig|1423792.3.peg.1323; -.
DR   OrthoDB; 9801717at2; -.
DR   Proteomes; UP000051330; 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   SUPFAM; SSF47823; lambda integrase-like, N-terminal domain; 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}.
FT   DOMAIN          2..86
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          107..289
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        241
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        276
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
SQ   SEQUENCE   296 AA;  33627 MW;  B29FC659719D34E6 CRC64;
     MSREQDWVAD FSRFLQLDQG LAKNTRLSYC RDVRTFLSWL NEQHEPLPTS APVIEAFLQT
     QAAAGKAVQS QIRLVASLRK FYRFAIHQHL VAHDPMTLVD APKATHHLPD VLSIGEVQSV
     LAQPDTSKPL GMRDRAILEV LYATGMRVSE LTTLQLTQLH LDLGLVQVVG KGDRERIVPI
     GDTAVNWLEQ YLRDIRPGYL HGRDQTVFLN FHGNGLSRQS IWKMIKKYVA QAGIQKDVTP
     HTLRHSFATH LLENGADLRV VQELLGHADI ATTQIYTHIS KTRLLDVYAK YHPRYE
//
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