ID A0A2U3AED6_9BACL Unreviewed; 299 AA.
AC A0A2U3AED6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:STX09069.1};
GN ORFNames=NCTC10597_00739 {ECO:0000313|EMBL:STX09069.1};
OS Kurthia zopfii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1650 {ECO:0000313|EMBL:STX09069.1, ECO:0000313|Proteomes:UP000254330};
RN [1] {ECO:0000313|EMBL:STX09069.1, ECO:0000313|Proteomes:UP000254330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10597 {ECO:0000313|EMBL:STX09069.1,
RC ECO:0000313|Proteomes:UP000254330};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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:STX09069.1}.
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DR EMBL; UGNP01000001; STX09069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3AED6; -.
DR OrthoDB; 9801717at2; -.
DR Proteomes; UP000254330; 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: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 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 ACT_SITE 150
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 174
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 299 AA; 34982 MW; D9217A922380C5A3 CRC64;
MHINQNEALQ QFITYVQLEK NYSVLTTAAY EQDLKEFFAF LSEEGIDRLE EVEYLHARLY
VTKLYNEQKA RATISRKISS IRSFFRFLNR DFELDDAPFQ ALYHPKKESR LPRFFYEEEL
KVLFEANKGE TPKEIRELAL LELLYATGIR VSELVSIELK DVDFSLSIIR VMGKGRKERY
VPFGQFAHEA MELYVNEARP ILMKKQQHET LFVNMKGLPL TARGVRYILN DVVEKSDLTA
KIHPHMIRHT FATHLLNNGA DLRTVQELLG HASLSSTQVY THITNEHLRK TYMNAHPRA
//
