XERC_RHOCS
ID XERC_RHOCS Reviewed; 341 AA.
AC B6IPE2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=RC1_2257;
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW;
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-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; CP000613; ACI99644.1; -; Genomic_DNA.
DR RefSeq; WP_012567429.1; NC_011420.2.
DR AlphaFoldDB; B6IPE2; -.
DR SMR; B6IPE2; -.
DR STRING; 414684.RC1_2257; -.
DR EnsemblBacteria; ACI99644; ACI99644; RC1_2257.
DR KEGG; rce:RC1_2257; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_5; -.
DR OMA; ERMVYFD; -.
DR OrthoDB; 745068at2; -.
DR Proteomes; UP000001591; 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..341
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000215957"
FT DOMAIN 14..105
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 126..309
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 169
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 193
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 261
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 296
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 341 AA; 36481 MW; 5A5155D372C40849 CRC64;
MTGGVPSLGF ACQPDAAEAL ERWGRWLEHE RGASTHTLRS YRADLAGFLA FVAEHRGRPP
GLNDLGALDL GAFRAWLAAR AADGAGAATR SRGVSGVRSF FRWADRSGLL HNPAIALLTA
PKAQRPLPRP LAADDAALLL EEAAAVPEAP WIGLRDRALF TLLYGCGLRI SEAIGLNRSD
LPAGAASVRV LGKGGKQRDV PVLPAVREAV AAYLAAVPWG GGRAAPLFVG AKGDRLSPDV
ARRQMRHLRA LLGLPDSTTP HALRHSFATH LLGGGADLRA IQDLLGHASL STTQRYTDVD
AEHLLSVYET AHPRARRQGH QTVRSVCDAL PPRLRNQESE R