XERD_SALTI
ID XERD_SALTI Reviewed; 298 AA.
AC P0A2P7; P55889;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Tyrosine recombinase XerD;
GN Name=xerD; OrderedLocusNames=STY3200, t2962;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC the cutting and rejoining of the recombining DNA molecules. Binds
CC cooperatively to specific DNA consensus sequences that are separated
CC from XerC binding sites by a short central region, forming the
CC heterotetrameric XerC-XerD complex that recombines DNA substrates. The
CC complex is essential to convert dimers of the bacterial chromosome into
CC monomers to permit their segregation at cell division. It also
CC contributes to the segregational stability of plasmids. In the complex
CC XerD specifically exchanges the bottom DNA strands (By similarity).
CC {ECO:0000250}.
CC -!- ACTIVITY REGULATION: FtsK may regulate the catalytic switch between
CC XerC and XerD in the heterotetrameric complex during the two steps of
CC the recombination process. {ECO:0000250}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD, in which XerC interacts
CC with XerD via its C-terminal region, XerD interacts with XerC via its
CC C-terminal region and so on. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.
CC {ECO:0000305}.
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; AL513382; CAD02874.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70514.1; -; Genomic_DNA.
DR RefSeq; NP_457442.1; NC_003198.1.
DR RefSeq; WP_000434302.1; NZ_WSUR01000024.1.
DR AlphaFoldDB; P0A2P7; -.
DR SMR; P0A2P7; -.
DR STRING; 220341.16504127; -.
DR EnsemblBacteria; AAO70514; AAO70514; t2962.
DR KEGG; stt:t2962; -.
DR KEGG; sty:STY3200; -.
DR PATRIC; fig|220341.7.peg.3258; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; QAFWYLI; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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.
FT CHAIN 1..298
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095412"
FT DOMAIN 2..87
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 108..292
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 279
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
SQ SEQUENCE 298 AA; 34220 MW; 15EF1040966DA25E CRC64;
MEQDLARIEQ FLDALWLERN LAENTLSAYR RDLSMVVAWL HHRGKTLATA QADDLQTLLA
ERVEGGYKAT SSARLLSAMR RFFQHLYREK YREDDPSAQL ASPKLPQRLP KDLSEAQVER
LLQAPLIDQP LELRDKAMLE VLYATGLRVS ELVGLTMSDI SLRQGVVRVI GKGNKERLVP
LGEEAVYWLE TYLEHGRPWL LNGVSIDVLF PSQRAQQMTR QTFWHRIKHY AVLAGIDSEK
LSPHVLRHAF ATHLLNHGAD LRVVQMLLGH SDLSTTQIYT HVATERLRQL HQQHHPRA
