XERC_PSEPG
ID XERC_PSEPG Reviewed; 299 AA.
AC B0KQ43;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN OrderedLocusNames=PputGB1_5291;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABZ01173.1; -; Genomic_DNA.
DR RefSeq; WP_012274782.1; NC_010322.1.
DR AlphaFoldDB; B0KQ43; -.
DR SMR; B0KQ43; -.
DR STRING; 76869.PputGB1_5291; -.
DR EnsemblBacteria; ABZ01173; ABZ01173; PputGB1_5291.
DR KEGG; ppg:PputGB1_5291; -.
DR eggNOG; COG4973; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000002157; 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; IPR011931; Recomb_XerC.
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 TIGRFAMs; TIGR02224; recomb_XerC; 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..299
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000088242"
FT DOMAIN 1..85
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 106..285
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 237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 240
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 263
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 272
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 299 AA; 33811 MW; B01DBD27E9B67659 CRC64;
MERQLEAYCA HLRNERQVSE HTLLGYRRDL DKVIAYCKEH GIADWQALQI QQLRQLIARL
HHHGQSSRSL ARLLSAVRGL YRYLNREGLC QHDPATGLSA PKGERRLPKV LDTDRALQLL
DGGVDDDFIA RRDQAILELF YSSGLRLSEL TNLDLDHLDL AAGLVQVLGK GGKARVLPVG
RKAREALQAW YRLRGIGNPR DRAVFITRQG NRISPQAVRL RVKAAGEREL GQHLHPHMLR
HSFASHVLES SQDLRAVQEL LGHADISTTQ IYTHLDFQHL AAVYDSAHPR AKRSKGNDS