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Database: UniProt
Entry: E1VVU4_GLUAR
LinkDB: E1VVU4_GLUAR
Original site: E1VVU4_GLUAR 
ID   E1VVU4_GLUAR            Unreviewed;       334 AA.
AC   E1VVU4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808,
GN   ECO:0000313|EMBL:CBT75747.1};
GN   OrderedLocusNames=AARI_15240 {ECO:0000313|EMBL:CBT75747.1};
OS   Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS   JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN   [1] {ECO:0000313|EMBL:CBT75747.1, ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RX   PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA   Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA   Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA   Vallaeys T.;
RT   "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT   adaptation to the surface of cheese.";
RL   PLoS ONE 5:E15489-E15489(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RA   Genoscope.;
RT   "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT   CIP 108037 / JCM 13566 / Re117).";
RL   Submitted (JUL-2010) 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:0000256|HAMAP-Rule:MF_01808}.
CC   -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC       molecules of XerC and two molecules of XerD. {ECO:0000256|HAMAP-
CC       Rule:MF_01808}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01808}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01808}.
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DR   EMBL; FQ311875; CBT75747.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1VVU4; -.
DR   STRING; 861360.AARI_15240; -.
DR   KEGG; aai:AARI_15240; -.
DR   eggNOG; COG4974; Bacteria.
DR   HOGENOM; CLU_027562_9_0_11; -.
DR   Proteomes; UP000006878; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-UniRule.
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:DNA transposition; IEA:UniProtKB-UniRule.
DR   CDD; cd00798; INT_XerDC_C; 1.
DR   Gene3D; 1.10.150.130; -; 1.
DR   Gene3D; 1.10.443.10; Intergrase catalytic core; 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   PANTHER; PTHR30349:SF41; INTEGRASE_RECOMBINASE HI_1414-RELATED; 1.
DR   PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR   Pfam; PF02899; Phage_int_SAM_1; 1.
DR   Pfam; PF00589; Phage_integrase; 1.
DR   SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR   PROSITE; PS51900; CB; 1.
DR   PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01808};
KW   DNA integration {ECO:0000256|ARBA:ARBA00022908, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01808}; Reference proteome {ECO:0000313|Proteomes:UP000006878}.
FT   DOMAIN          17..104
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          125..328
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        315
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   334 AA;  37574 MW;  82B04864EFACCB61 CRC64;
     MVMKHDPVSK HSTGPSAKFS EPVADYLEYL QRERGRSENT LRAYDVDLRN LGQFLNEHAG
     DPALKQISVQ MLRDWLAYLH ESEVSRTTLA RRISAVKNFF AWALKNHLVE NDPALRLAAP
     KKERRLPHIL QPSQIDRLLS EHAGLTEENE AARQKGDGTD QDPKARAIQC RDRVIAELLY
     ASGLRISELV ALDISDIDFE RRTLRVLGKG NKERMVPFGK PAERVIIEWI RSYRRVVAAE
     QAEDALLVGV RGSRLNVRQA REVIASALRS LGDTSASGPH ALRHTVATHL LDGGADLRAV
     QEFLGHASLA TTQLYTHVSV DRLRQSYRQA HPRA
//
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