ID A0A3T1AN70_9ACTN Unreviewed; 329 AA.
AC A0A3T1AN70;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerC_1 {ECO:0000313|EMBL:BBH64348.1};
GN Synonyms=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN ORFNames=ACTI_10330 {ECO:0000313|EMBL:BBH64348.1};
OS Actinoplanes sp. OR16.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=946334 {ECO:0000313|EMBL:BBH64348.1, ECO:0000313|Proteomes:UP000282692};
RN [1] {ECO:0000313|EMBL:BBH64348.1, ECO:0000313|Proteomes:UP000282692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:BBH64348.1,
RC ECO:0000313|Proteomes:UP000282692};
RA Kasai D.;
RT "Complete genome sequence of natural rubber degrading Actinoplanes sp.
RT strain OR16 isolated form botanical garden in Japan.";
RL Submitted (DEC-2018) 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; AP019371; BBH64348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T1AN70; -.
DR Proteomes; UP000282692; 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 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 12..98
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 141..323
FT /note="Tyr recombinase"
FT /evidence="ECO:0000259|PROSITE:PS51898"
FT REGION 134..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 205
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 301
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 310
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 329 AA; 35920 MW; 4DDA4D2BB71F90BA CRC64;
MRTRQLHEAL PPTLRQAVDD FGQHLAGVEN RSEHTVRAYL GDVVSLLDHA VREGRYGLDD
LDITVLRGWL AARMGEGAAR TSQARRAAAA RAFTGWAHRA GRASDDPGAQ LASPRAHRNL
PAVLRADQAE ALVTQQSAKH RPKDRQETAE DERQAAEDRP ATPEGIRDRA VLEMLYATGI
RVSELCGLNR ADVDHGRQVV RVFGKGAKER AVPYGHPARD ALDLWLRAGW PELANRLSRD
ALFLGAKGGR LQPTVVRRIV AGAARAAGLP HTSPHDLRHS AATHLLDGGA DLRAVQELLG
HSSLSSTQIY THVSTERLRA AFKQAHPRA
//
