ID A0A418XKG3_9PSED Unreviewed; 346 AA.
AC A0A418XKG3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|ARBA:ARBA00015804, ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808,
GN ECO:0000313|EMBL:RJG12947.1};
GN ORFNames=D3879_06630 {ECO:0000313|EMBL:RJG12947.1};
OS Pseudomonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2320866 {ECO:0000313|EMBL:RJG12947.1, ECO:0000313|Proteomes:UP000284021};
RN [1] {ECO:0000313|EMBL:RJG12947.1, ECO:0000313|Proteomes:UP000284021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-6 {ECO:0000313|EMBL:RJG12947.1,
RC ECO:0000313|Proteomes:UP000284021};
RA Zhu H.;
RL Submitted (SEP-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|ARBA:ARBA00006657, 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:RJG12947.1}.
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DR EMBL; QYUR01000002; RJG12947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418XKG3; -.
DR OrthoDB; 9801717at2; -.
DR Proteomes; UP000284021; 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; IPR011931; Recomb_XerC.
DR InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR NCBIfam; TIGR02224; recomb_XerC; 1.
DR PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR PANTHER; PTHR30349:SF85; TYROSINE RECOMBINASE XERC; 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..85
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 106..285
FT /note="Tyr recombinase"
FT /evidence="ECO:0000259|PROSITE:PS51898"
FT REGION 289..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 170
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 237
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 240
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 263
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 272
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 346 AA; 38488 MW; 4EB1B0DCEDCB50BB CRC64;
MQACLDAYLE HLRSERQMSP NTLAAYRRDL LKLLELCDQQ AIAEWAKLDV RSLRSFIARL
HQQGLSGRSL ARLLSATRGL YQFLIGQGIC LHDPASGVSP PKRERRLPRT LDADRALQLL
DGAVEDDFIA RRDQAILELF YSSGLRLSEL TGLNLQQLDL ADGLVQVLGK GGKQRVLPVG
RMARQALENW LPLRALANPS DGAVFISQQG RRLGPRAIQL RVRQAGVREL GQHLHPHMLR
HSFASHMLES SQDLRAVQEL LGHADIATTQ IYTHLDFQHL AAVYDSAHPR AKRAKAGQRE
SVPSEDGTRQ KQVKPQSLQS VNEQAEPAFN ARSTSAAALA LPEKTK
//
