ID Q6F952_ACIAD Unreviewed; 305 AA.
AC Q6F952;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808,
GN ECO:0000313|EMBL:CAG69413.1};
GN OrderedLocusNames=ACIAD2657 {ECO:0000313|EMBL:CAG69413.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG69413.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG69413.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG69413.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F952; -.
DR STRING; 202950.GCA_001485005_02303; -.
DR KEGG; aci:ACIAD2657; -.
DR eggNOG; COG4973; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OrthoDB; 9801717at2; -.
DR BioCyc; ASP62977:ACIAD_RS12080-MONOMER; -.
DR Proteomes; UP000000430; 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 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:UP000000430}.
FT DOMAIN 2..87
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 108..295
FT /note="Tyr recombinase"
FT /evidence="ECO:0000259|PROSITE:PS51898"
FT ACT_SITE 152
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 176
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 247
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 250
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 273
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 282
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 305 AA; 35595 MW; 57CF4B77630A0BBD CRC64;
MYNNQQLLAM WLKERMIQNQ SEHTLNAYQR DLTDFFDFCE KRKLELMQVE ASDLREYLAY
RVEQSNLSSS SIQRHLSSIR QFMKWAQQSQ FLNMNPVEDF KLKRKSRPLP GMIDIETVHQ
ILDQTAPEDE LGTQLWLRDK AILELLYSSG LRLAELQGLK LIDLDFNRQL LRVTGKGNKT
RVIPFGKKAK QSLIDWLNVY RLWKGQFTQQ DPLFVSQNGG ALTPRQIENR VKHQALRAGV
NVDLHPHLLR HCFASHMLSA SGDLRSVQEM LGHSNLSTTQ IYTHIDFDHL AQVYDRAHPR
AQKIK
//