XERC_ERYLH
ID XERC_ERYLH Reviewed; 306 AA.
AC Q2NB52;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=ELI_04985;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC63089.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NB52; -.
DR SMR; Q2NB52; -.
DR STRING; 314225.ELI_04985; -.
DR EnsemblBacteria; ABC63089; ABC63089; ELI_04985.
DR KEGG; eli:ELI_04985; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_5; -.
DR OMA; HRFLYAE; -.
DR Proteomes; UP000008808; 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; 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; Reference proteome.
FT CHAIN 1..306
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000070004"
FT DOMAIN 2..81
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 102..283
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 146
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 235
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 238
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 261
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 270
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 306 AA; 33284 MW; E275DE1D9DAEE889 CRC64;
MAKASAAIEE FLAMLAAERG AAANTLAAYR RDLEGAEALA GDLATARRPA LSRLGSAWSD
LAPATVARKA SALRQFYGFL VDEGLREDDP SSALPRPTMR RPLPKTLSHK EVERLFEQAE
REAETSRPLP VRLLALIELL YGSGLRATEL VSLPVAAVPR DAPFLTVTGK GGVARMVPVS
GRAREALQSW MGLRGSDSPY LFPSRKAHIT RVRLFQMLKE LAVRADLNPD KVSPHVLRHA
FATHLLEGGA DLRVLQTLLG HADISTTQIY THVDAARLVA LVNERHPLSA RAAGKRSTLA
EKRTED