ID A0A0S9DRU4_9MICO Unreviewed; 305 AA.
AC A0A0S9DRU4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN ORFNames=ASF06_10685 {ECO:0000313|EMBL:KQO08615.1};
OS Agreia sp. Leaf244.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agreia.
OX NCBI_TaxID=1736305 {ECO:0000313|EMBL:KQO08615.1, ECO:0000313|Proteomes:UP000051484};
RN [1] {ECO:0000313|EMBL:KQO08615.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO08615.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO08615.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO08615.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQO08615.1}.
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DR EMBL; LMLX01000003; KQO08615.1; -; Genomic_DNA.
DR RefSeq; WP_055946730.1; NZ_LMLX01000003.1.
DR AlphaFoldDB; A0A0S9DRU4; -.
DR STRING; 1736305.ASF06_10685; -.
DR OrthoDB; 9801717at2; -.
DR Proteomes; UP000051484; Unassembled WGS sequence.
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 SUPFAM; SSF47823; lambda integrase-like, N-terminal domain; 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}.
FT DOMAIN 1..87
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 108..299
FT /note="Tyr recombinase"
FT /evidence="ECO:0000259|PROSITE:PS51898"
FT ACT_SITE 152
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 176
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 251
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 254
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 277
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 286
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 305 AA; 33249 MW; 6EE45AAFD0011DC2 CRC64;
MKLERAIDDF VSYLTAERGY SPHTVRAYRS DLASLSGFAQ SRGIDDAAQL TLDAYRDWLW
TASQAGLSKA TLARRSATAK SFSSWFTRSN GKALDAASRL RAPKPDRSLP RVLSRDAMDS
VLDSLVARTH EGEPLALRDL AIVELLYASA LRVSELVGID TTDLDLDRRT VRVLGKGSKE
RVVPFGQPAH LALVDYLQRG RPALAARSEE SSGTRAVFLG ARGARVGTRS VYGIVSKLLM
DVPGSGPEGP HAFRHTAATH LLDGGADLRA VQEMLGHASL GTTQIYTHVT TERLRETYRQ
AHPRA
//
