XERC_RICFE
ID XERC_RICFE Reviewed; 305 AA.
AC Q4UJZ3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=RF_1295;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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; CP000053; AAY62146.1; -; Genomic_DNA.
DR RefSeq; WP_011271595.1; NC_007109.1.
DR AlphaFoldDB; Q4UJZ3; -.
DR SMR; Q4UJZ3; -.
DR STRING; 315456.RF_1295; -.
DR PRIDE; Q4UJZ3; -.
DR EnsemblBacteria; AAY62146; AAY62146; RF_1295.
DR KEGG; rfe:RF_1295; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_5; -.
DR OMA; QVYAHIG; -.
DR OrthoDB; 745068at2; -.
DR Proteomes; UP000008548; 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.
FT CHAIN 1..305
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_0000272366"
FT DOMAIN 4..95
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 116..298
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 159
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 182
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 253
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 285
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 305 AA; 35486 MW; F52E452CA12F7848 CRC64;
MLDTSIQELI DKWQKYLDLQ RNYSNHTVIS YNNDLKHFLE FMNYYNSELV TINHIKTADI
RLIRSWLAKR NCDNFTTSSI SRGLSAVKNF YRFLEKTTQL NSHIIFSIKS PKKTKLLPKA
LSEDDVVISL EHIEEYGNVK WVELRNKALL VLIYASGLRI SEALSITKLH LQNLEFIRII
GKGSKERIIP WLPIAKNLIT QYLEILPYKL GDNEPIFRGK QGKKLQPPVF NRELIKLKHF
YGLPQHLTAH SFRHSFASHL LEHGADLRSI QELLGHKSLS TTQNYTKTSI KHLEAVYTTA
YPIKK