ID   XERD_CHLMU              Reviewed;         301 AA.
AC   Q9PL53;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN   Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; OrderedLocusNames=TC_0255;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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:0000255|HAMAP-Rule:MF_01807}.
CC   -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC       molecules of XerC and two molecules of XerD. {ECO:0000255|HAMAP-
CC       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; AE002160; AAF39124.1; -; Genomic_DNA.
DR   PIR; A81724; A81724.
DR   AlphaFoldDB; Q9PL53; -.
DR   SMR; Q9PL53; -.
DR   STRING; 243161.TC_0255; -.
DR   EnsemblBacteria; AAF39124; AAF39124; TC_0255.
DR   KEGG; cmu:TC_0255; -.
DR   eggNOG; COG4974; Bacteria.
DR   HOGENOM; CLU_027562_9_6_0; -.
DR   OMA; HRFLYAE; -.
DR   Proteomes; UP000000800; 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   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..301
FT                   /note="Tyrosine recombinase XerD"
FT                   /id="PRO_0000095379"
FT   DOMAIN          6..89
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          108..293
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT   ACT_SITE        280
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ   SEQUENCE   301 AA;  34887 MW;  0F078DD86453D6E9 CRC64;
     MSMLFPLHQQ LIEQFTIFLS VDRGIAPLSV QAYCQDILLF LQRVPIETTD MINQESVFLF
     VEKCHQAKES ETTLARRLIA LKVFFHFLKD AKLIHQQPFI EHPKVWKRLP SILSTEEVNS
     LLNQPLNTLN LDAYIANRDT AILYTFYATG IRVSELCDLC IGDISDDFIR VTGKGRKTRL
     VPISIKARQT IDSYLTMFRE RFQKKNPSEE HVFLSIRGKK LERSCVWKRI TFYAKLVTTK
     HISPHSLRHA FATHLLNNQA DLRIIQEMLG HARISSTEIY THVASESIIE KFHTHHPRSS
     S