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Database: UniProt
Entry: L1PAT8_9FLAO
LinkDB: L1PAT8_9FLAO
Original site: L1PAT8_9FLAO 
ID   L1PAT8_9FLAO            Unreviewed;       303 AA.
AC   L1PAT8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   ORFNames=HMPREF9075_00300 {ECO:0000313|EMBL:EKY12585.1};
OS   Capnocytophaga sp. oral taxon 332 str. F0381.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1127692 {ECO:0000313|EMBL:EKY12585.1, ECO:0000313|Proteomes:UP000010419};
RN   [1] {ECO:0000313|EMBL:EKY12585.1, ECO:0000313|Proteomes:UP000010419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0381 {ECO:0000313|EMBL:EKY12585.1,
RC   ECO:0000313|Proteomes:UP000010419};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) 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   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.
CC       {ECO:0000256|ARBA:ARBA00010450}.
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:EKY12585.1}.
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DR   EMBL; AMET01000022; EKY12585.1; -; Genomic_DNA.
DR   RefSeq; WP_009416523.1; NZ_KB291341.1.
DR   AlphaFoldDB; L1PAT8; -.
DR   STRING; 1127692.HMPREF9075_00300; -.
DR   PATRIC; fig|1127692.3.peg.282; -.
DR   eggNOG; COG4974; Bacteria.
DR   HOGENOM; CLU_027562_9_6_10; -.
DR   OrthoDB; 9801717at2; -.
DR   Proteomes; UP000010419; 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; IPR011932; Recomb_XerD.
DR   InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR   NCBIfam; TIGR02225; recomb_XerD; 1.
DR   PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR   PANTHER; PTHR30349:SF87; PROPHAGE INTEGRASE INTD-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}; Reference proteome {ECO:0000313|Proteomes:UP000010419}.
FT   DOMAIN          1..86
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          107..291
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        278
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   303 AA;  35575 MW;  A71DEF9843FAB180 CRC64;
     MWQSANTDFQ HYLRFQRGLS QNTVTSYGLD IEKLINYLQK YHITETPDNI TEDTLRQFIY
     QEGKLLNARS QARLISSLKG FFKFMMYEKG REDFPMSLID SPKIGLKLPD TLSLQEIDTL
     LNSIDLSTDE GHRNKAIIEI LYACGLRVSE LVNLRLSDLF FEEDFIRIVG KGSKQRLVPI
     EKYTQRQVKN YIDNQRKYLK IAKGHEDYVF LNRRGQQLTR AMIFTIVRRT AECVGLQKKI
     SPHTFRHSFA THLLENGANL RAIQMMLGHE NITTTEIYIH VERGYLREVL EKFHPRQKMS
     FTQ
//
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