ID A0A1Y5R8D0_9RHOB Unreviewed; 301 AA.
AC A0A1Y5R8D0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerD {ECO:0000313|EMBL:SLN10433.1};
GN Synonyms=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN ORFNames=PAM7066_00023 {ECO:0000313|EMBL:SLN10433.1};
OS Palleronia marisminoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=315423 {ECO:0000313|EMBL:SLN10433.1, ECO:0000313|Proteomes:UP000193870};
RN [1] {ECO:0000313|EMBL:SLN10433.1, ECO:0000313|Proteomes:UP000193870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7066 {ECO:0000313|EMBL:SLN10433.1,
RC ECO:0000313|Proteomes:UP000193870};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFV01000001; SLN10433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5R8D0; -.
DR STRING; 315423.SAMN04488020_10123; -.
DR OrthoDB; 9801717at2; -.
DR Proteomes; UP000193870; 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 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; 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 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:UP000193870}.
FT DOMAIN 1..84
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 105..293
FT /note="Tyr recombinase"
FT /evidence="ECO:0000259|PROSITE:PS51898"
FT ACT_SITE 148
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 172
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 245
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 248
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 271
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 280
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 301 AA; 33417 MW; 9675D59BCCF5F889 CRC64;
MSLARQIATF IEARVAEMGA AENTRLAYAR DLSDFSTWIA AESAASVTRD RIEAYLIHCE
AQGFAVSTRA RRLSAIKGFF RFAYEEGWRE DNPAIRIKGP GRERRLPKTI EVEDVDRLID
AAGRTGRAEC DRRRNTCLLE LLYATGMRVT ELVSLPVSAA RGDPRMLLIS GKGGKERMVP
LTDGAREALS DWLTTRDAAE DPRAPSRFLF PSRGKAGHLT RHRFFQLIKE IALEAGLAPD
EITPHTLRHA FATHLLAGGA DLMAIQALLG HADVATTEIY THVLDQRLRE LVLDHHPLAK
G
//
