XERC_HAEDU
ID XERC_HAEDU Reviewed; 304 AA.
AC Q7VKG8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=HD_1940;
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_01808}.
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_01808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01808}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01808}.
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DR EMBL; AE017143; AAP96660.1; -; Genomic_DNA.
DR RefSeq; WP_010945687.1; NC_002940.2.
DR AlphaFoldDB; Q7VKG8; -.
DR SMR; Q7VKG8; -.
DR STRING; 233412.HD_1940; -.
DR EnsemblBacteria; AAP96660; AAP96660; HD_1940.
DR KEGG; hdu:HD_1940; -.
DR eggNOG; COG4973; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; HSFASHM; -.
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 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; IPR011931; Recomb_XerC.
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; TIGR02224; recomb_XerC; 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..304
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_0000095297"
FT DOMAIN 6..92
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 113..292
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 152
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 176
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 247
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 270
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 279
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 304 AA; 34819 MW; D6A414CF93ACD06D CRC64;
MLNKQNKLYL QAQAYWDFLR IEKQVSPHTL TNYQRQLLAI SEMLIAAQID DWQAVDASVV
RWILTQSHKQ GLGAKSIGLR LVVLRQWFAY LVQRHYVKVN PAVGIKAPKV ARHLPKNIDA
ERMGQLLDVE VDEPADIRDL AMMELMYSSG LRLAELQRLD LGDMDLIDAE VRLLGKGNKE
RIVPIGSRAL TALQAWLTVR PSFNPQDNAL FLNKRGGRLS HRSIQLAMQK WGERQGLATR
LHPHKLRHSF ATHLLEASTD LRAVQELLGH SSLSTTQIYT HLDFQHLAKI YDASHPRARR
KRED