XERC_RICAH
ID XERC_RICAH Reviewed; 305 AA.
AC A8GQ15;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=A1C_06315;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) 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; CP000847; ABV75490.1; -; Genomic_DNA.
DR RefSeq; WP_012150119.1; NC_009881.1.
DR AlphaFoldDB; A8GQ15; -.
DR SMR; A8GQ15; -.
DR STRING; 293614.A1C_06315; -.
DR EnsemblBacteria; ABV75490; ABV75490; A1C_06315.
DR KEGG; rak:A1C_06315; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_5; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000006830; 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_1000070032"
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; 35682 MW; B5F55E3AA08797D4 CRC64;
MLDILIQELI DKWQKYLVLQ RNYSNYTVIS YNNDLKNFLE FMNYYNSELV TINHIKNADI
RLIRSWLAKR NYDNFTTSSI ARGLSAVKNF YRFLEKTTQL NSHIIFSIKS PKKTKLLPKA
LSEDDVVVSL EHIEEYGNVK WVELRNKSLL VLIYASGLRI SEALSITKLH LQNLEFIRII
GKGSKERIIP WLPIAKNLIT QYLEILPYKL GDNEPIFRGK RGKKLQPQVF NRELIKLKHF
YGLPQHLTAH SFRHSFASHL LERGAELRSI QELLGHKSLS TTQNYTKTSI KRLEAVYTTA
YPIKK