XERD_HAEDU
ID XERD_HAEDU Reviewed; 297 AA.
AC Q7VPN8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807};
GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; OrderedLocusNames=HD_0013;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP95036.1; -; Genomic_DNA.
DR RefSeq; WP_010944090.1; NC_002940.2.
DR AlphaFoldDB; Q7VPN8; -.
DR SMR; Q7VPN8; -.
DR STRING; 233412.HD_0013; -.
DR EnsemblBacteria; AAP95036; AAP95036; HD_0013.
DR KEGG; hdu:HD_0013; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; QAFWYLI; -.
DR Proteomes; UP000001022; 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..297
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095389"
FT DOMAIN 2..86
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 107..291
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 171
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 269
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
FT ACT_SITE 278
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01807"
SQ SEQUENCE 297 AA; 34472 MW; 589A1B3984E73951 CRC64;
MKKLDPIIEQ FLDTLWLEQS LSHNTLLSYR LDLELFSAWL VEPRAFLTLT HTDLQLFLGD
RLDKGYKSSS SARIISCLRK FFRFLCLEKY RLDDPTSMLI SPRKRVQLPK SLSEEQVMDL
LDAPNPLDPI ELRDKAMLEL LYATGLRVTE LISLTIDNLN LRQGVVRVIG KGDKERLVPI
GEEASYWIQE FFDYGRMILL SDQQSDVLFP SRRAKQMTRQ TFWHRIKYYA ILAGIDAEKL
SPHVLRHAFA THLINHGADL RVVQMLLGHS DLSTTQIYTH VAKTRLKSIH KQFHPRG