ID A0A1I7GKX7_9BURK Unreviewed; 323 AA.
AC A0A1I7GKX7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN ORFNames=SAMN04489707_10062 {ECO:0000313|EMBL:SFU49001.1};
OS Paenacidovorax caeni.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paenacidovorax.
OX NCBI_TaxID=343013 {ECO:0000313|EMBL:SFU49001.1, ECO:0000313|Proteomes:UP000183656};
RN [1] {ECO:0000313|EMBL:SFU49001.1, ECO:0000313|Proteomes:UP000183656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-24608 {ECO:0000313|EMBL:SFU49001.1,
RC ECO:0000313|Proteomes:UP000183656};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FPBX01000006; SFU49001.1; -; Genomic_DNA.
DR RefSeq; WP_054257187.1; NZ_FPBX01000006.1.
DR AlphaFoldDB; A0A1I7GKX7; -.
DR STRING; 343013.SAMN04489707_10062; -.
DR OrthoDB; 9801717at2; -.
DR Proteomes; UP000183656; 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: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 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:UP000183656}.
FT DOMAIN 5..93
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 114..310
FT /note="Tyr recombinase"
FT /evidence="ECO:0000259|PROSITE:PS51898"
FT ACT_SITE 156
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 191
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 262
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 265
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 288
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 297
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 323 AA; 35279 MW; B6B5472C0415A1C2 CRC64;
MPPPNTPPEL PDEALRYLEH VRVEKRLAAR TLALYTQDLL RLHQYAQAVG LPLLLLTSGH
LRRFVAQMHG GGRSARGIVL ILSGWRGFYR WAARQGLTAH NPAQGLRAPK APKPLPKALA
VDDAVRLADF AQPGDDPWVE ARDAAMVELL YGCGLRVGEL VGLDVAASPA AHQQGRGWID
LDAAEAHVFG KGSKRRSLPV GRAALAALRA WLALREQPFG ARLADGALFV GRRGARLSAA
SVWARLRQRG QQAGLSTPVH PHMLRHSFAS HLLQSSGDLR AVQELLGHAS ITTTQAYTRL
DFQHLARVYD QAHPRAKKKP SPL
//
