XERC_RICAE
ID XERC_RICAE Reviewed; 305 AA.
AC C3PLU8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=RAF_ORF1159;
OS Rickettsia africae (strain ESF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=347255;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESF-5;
RX PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT "Analysis of the Rickettsia africae genome reveals that virulence
RT acquisition in Rickettsia species may be explained by genome reduction.";
RL BMC Genomics 10:166-166(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; CP001612; ACP53938.1; -; Genomic_DNA.
DR RefSeq; WP_012720064.1; NC_012633.1.
DR AlphaFoldDB; C3PLU8; -.
DR SMR; C3PLU8; -.
DR EnsemblBacteria; ACP53938; ACP53938; RAF_ORF1159.
DR KEGG; raf:RAF_ORF1159; -.
DR HOGENOM; CLU_027562_9_0_5; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000002305; 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_1000215958"
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; 35368 MW; 4C4EF640C6113E96 CRC64;
MLDTSIQALI NKWQKYLVLQ RNYSNHTVIS YNNDLKHFLE FMNYYNSELV TINHIKTADI
RLIRSWLAKR NCDNFTASSI SRGLSAVKNF YRFLEKTTQL NSHIIFSIKS PKKTKLLPKA
LSEDDVVISL EHIEEYGNVK WIELRNKALL VLIYASGLRI SEALSITKLH LQNLEFIRII
GKGSKERIIP WLPIAKNLIT QYLEILPYKL GDNEPIFRGK QGKKLQPPVF NRELIKLKHF
YGLPQHLTAH SFRHSFASHL LEHGADLRSL QELLGHKSLS TTQSYTKTSI KHLEAVYTTA
YPIKK