XERC_MYCSK
ID XERC_MYCSK Reviewed; 300 AA.
AC A1UEH7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=Mkms_2036;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) 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; CP000518; ABL91235.1; -; Genomic_DNA.
DR RefSeq; WP_011559389.1; NC_008705.1.
DR AlphaFoldDB; A1UEH7; -.
DR SMR; A1UEH7; -.
DR STRING; 189918.Mkms_2036; -.
DR EnsemblBacteria; ABL91235; ABL91235; Mkms_2036.
DR KEGG; mkm:Mkms_2036; -.
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_1000070015"
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; 32429 MW; 7E7A4C4D78D2F961 CRC64;
MESVLDAFDQ YLALERGRSD HTRRAYLGDL RSLFAFCNER TPGADLGSLT LPVLRAWLSA
QAAAGTARTT LARRTSAVKT FTAWAVRRGL MASDPATRLQ MPKARRTLPA VLRQDQARDA
LDAANSGAQQ GDPLALRDRL IVEMLYATGI RVSELCGLDI DDVDTSRRLL RVLGKGDKQR
TVPFGEPAEQ ALRAWLTSGR PALATAESGP ALLLGARGRR LDPRQARTVV HETVGAVAGA
PDIGPHGLRH SAATHLLEGG ADLRIVQELL GHSTLATTQL YTHVTVARLR AVHDQAHPRA