XERD_SALTY
ID XERD_SALTY Reviewed; 298 AA.
AC P0A2P6; P55889;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tyrosine recombinase XerD;
GN Name=xerD; OrderedLocusNames=STM3044;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=9370270; DOI=10.1016/s0378-1119(97)00299-0;
RA Hayes F., Lubetzki S.A., Sherratt D.J.;
RT "Salmonella typhimurium specifies a circular chromosome dimer resolution
RT system which is homologous to the Xer site-specific recombination system of
RT Escherichia coli.";
RL Gene 198:105-110(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLY-171; LYS-172; ARG-177; GLY-182 AND
RP ALA-185.
RX PubMed=10356326; DOI=10.1006/jmbi.1999.2793;
RA Cao Y., Hayes F.;
RT "A newly identified, essential catalytic residue in a critical secondary
RT structure element in the integrase family of site-specific recombinases is
RT conserved in a similar element in eucaryotic type IB topoisomerases.";
RL J. Mol. Biol. 289:517-527(1999).
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, ECO:0000269|PubMed:10356326}.
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}.
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DR EMBL; U92524; AAC45774.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21919.1; -; Genomic_DNA.
DR RefSeq; NP_461960.1; NC_003197.2.
DR RefSeq; WP_000434302.1; NC_003197.2.
DR AlphaFoldDB; P0A2P6; -.
DR SMR; P0A2P6; -.
DR STRING; 99287.STM3044; -.
DR PaxDb; P0A2P6; -.
DR EnsemblBacteria; AAL21919; AAL21919; STM3044.
DR GeneID; 1254567; -.
DR KEGG; stm:STM3044; -.
DR PATRIC; fig|99287.12.peg.3224; -.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; QAFWYLI; -.
DR PhylomeDB; P0A2P6; -.
DR BioCyc; SENT99287:STM3044-MON; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA integration; DNA recombination; DNA-binding; Reference proteome.
FT CHAIN 1..298
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095413"
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"
FT MUTAGEN 171
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:10356326"
FT MUTAGEN 171
FT /note="G->W: Abolishes recombinase activity."
FT /evidence="ECO:0000269|PubMed:10356326"
FT MUTAGEN 172
FT /note="K->A: Abolishes recombinase activity."
FT /evidence="ECO:0000269|PubMed:10356326"
FT MUTAGEN 177
FT /note="R->A: Abolishes plasmid resolution but not
FT chromosomal recombination."
FT /evidence="ECO:0000269|PubMed:10356326"
FT MUTAGEN 180
FT /note="P->W: Abolishes plasmid resolution but not
FT chromosomal recombination."
FT MUTAGEN 182
FT /note="G->A,W: Abolishes plasmid resolution but not
FT chromosomal recombination."
FT /evidence="ECO:0000269|PubMed:10356326"
FT MUTAGEN 185
FT /note="A->V: Abolishes plasmid resolution but not
FT chromosomal recombination."
FT /evidence="ECO:0000269|PubMed:10356326"
FT CONFLICT 71
FT /note="S -> T (in Ref. 1; AAC45774)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="Q -> E (in Ref. 1; AAC45774)"
FT /evidence="ECO:0000305"
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
