XERC_MYCGI
ID XERC_MYCGI Reviewed; 300 AA.
AC A4TEB1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, 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=Mflv_4135;
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-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; CP000656; ABP46605.1; -; Genomic_DNA.
DR RefSeq; WP_011894984.1; NC_009338.1.
DR AlphaFoldDB; A4TEB1; -.
DR SMR; A4TEB1; -.
DR STRING; 350054.Mflv_4135; -.
DR EnsemblBacteria; ABP46605; ABP46605; Mflv_4135.
DR KEGG; mgi:Mflv_4135; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_0_11; -.
DR OMA; QAFWYLI; -.
DR OrthoDB; 745068at2; -.
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..300
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000088239"
FT DOMAIN 1..86
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 107..294
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 151
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 272
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 281
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 300 AA; 32470 MW; B42C897349A048C0 CRC64;
MDTVLEEFDR YLELERGRSE HTRRAYLGDL RSLFAFLDER SPGTGLGGLT LPMLRSWLAA
HAAAGTARST LARRTSSVKT FTAWAVRRGL IGDDPASRLQ VPKARRTLPS VLRQDQARDA
LEAAESGAQQ GDPLAVRDRL VVEMLYATGI RVSELCGLDV DDVDTSRRLL RVLGKGNKQR
TVPYGEPAHA ALTAWLHEGR PALATADSGP ALLLGARGKR LDPRQARTVV HQTVSAVGGA
PDIGPHGLRH SAATHLLEGG ADLRVVQELL GHSSLATTQL YTHVTVARLR AVHDQAHPRA