ID   XNI_YERPA               Reviewed;         230 AA.
AC   Q1CAP8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Flap endonuclease Xni;
DE            Short=FEN;
DE            EC=3.1.-.-;
GN   Name=xni; Synonyms=ygdG; OrderedLocusNames=YPA_0506;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Has flap endonuclease activity. During DNA replication, flap
CC       endonucleases cleave the 5'-overhanging flap structure that is
CC       generated by displacement synthesis when DNA polymerase encounters the
CC       5'-end of a downstream Okazaki fragment (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 Mg(2+) per subunit. Only one magnesium ion has a direct
CC       interaction with the protein, the other interactions are indirect.
CC       {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC       Note=Binds 1 K(+) per subunit. The potassium ion strongly increases the
CC       affinity for DNA. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Xni family. {ECO:0000305}.
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DR   EMBL; CP000308; ABG12474.1; -; Genomic_DNA.
DR   RefSeq; WP_011566241.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1CAP8; -.
DR   SMR; Q1CAP8; -.
DR   EnsemblBacteria; ABG12474; ABG12474; YPA_0506.
DR   KEGG; ypa:YPA_0506; -.
DR   OMA; IEMARIC; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:InterPro.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR038969; FEN.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   PANTHER; PTHR42646; PTHR42646; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Potassium.
FT   CHAIN           1..230
FT                   /note="Flap endonuclease Xni"
FT                   /id="PRO_0000297894"
FT   DOMAIN          160..215
FT                   /note="5'-3' exonuclease"
FT   REGION          184..189
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   230 AA;  25585 MW;  ED566F0ED9D411DC CRC64;
     MQIHLLIVDA LNLIRRIHAV QGSPCVKACQ HALQQLIQHS QPSHAVAVFD EDDRSDSWRH
     QCLPDYKAGR SPMPDNLQQE MPLIRQAFNE LGVACWHSPG NEADDLAATL VVKVAGAGHQ
     VTIVSTDKGY CQLLAPNIQI RDYFQKRWLD MPFVKQEFGV LPRQLPDYWG LAGISSSKIP
     GVAGVGAKTA TLLLQQADTL EVLYQNLESI PECQRRMKSD PLISPPTAQY