ID   XERD_SHIFL              Reviewed;         298 AA.
AC   Q7ZAM0;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN   Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN   OrderedLocusNames=SF2880, S3079;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(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. {ECO:0000255|HAMAP-
CC       Rule:MF_01807}.
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:0000255|HAMAP-Rule:MF_01807}.
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:0000255|HAMAP-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; AE005674; AAN44365.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18187.1; -; Genomic_DNA.
DR   RefSeq; NP_708658.1; NC_004337.2.
DR   RefSeq; WP_000806987.1; NZ_WPGN01000021.1.
DR   AlphaFoldDB; Q7ZAM0; -.
DR   SMR; Q7ZAM0; -.
DR   STRING; 198214.SF2880; -.
DR   EnsemblBacteria; AAN44365; AAN44365; SF2880.
DR   EnsemblBacteria; AAP18187; AAP18187; S3079.
DR   GeneID; 1025811; -.
DR   KEGG; sfl:SF2880; -.
DR   KEGG; sft:NCTC1_03169; -.
DR   KEGG; sfx:S3079; -.
DR   PATRIC; fig|198214.7.peg.3427; -.
DR   HOGENOM; CLU_027562_9_0_6; -.
DR   OMA; QAFWYLI; -.
DR   OrthoDB; 745068at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..298
FT                   /note="Tyrosine recombinase XerD"
FT                   /id="PRO_0000095415"
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|HAMAP-Rule:MF_01807"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        279
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ   SEQUENCE   298 AA;  34260 MW;  0249D79420977384 CRC64;
     MKQELARIEQ FLDALWLEKN LAENTLNAYR RDLSMMVEWL HHRGLTLATA QSDDLQALLA
     ERLEGGYKAT SSARLLSAVR RLFQYLYREK FREDDPSAHL ASPKLPQRLP KDLSEAQVER
     LLQAPLIDQP LELRDKAMLE VLYATGLRVS ELVGLTMSDI SLRQGVVRVI GKGNKERLVP
     LGEEAVYWLE TYLEHGRPWL LNGVSIDVLF PSQRAQQMTR QTFWHRIKHY AVLAGIDSEK
     LSPHVLRHAF ATHLLNHGAD LRVVQMLLGH SDLSTTQIYT HVATERLRQL HQQHHPRA