ID   XNI_YERPG               Reviewed;         218 AA.
AC   A9R2J1;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Flap endonuclease Xni;
DE            Short=FEN;
DE            EC=3.1.-.-;
GN   Name=xni; Synonyms=ygdG; OrderedLocusNames=YpAngola_A3155;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX88088.1; -; Genomic_DNA.
DR   RefSeq; WP_012229894.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R2J1; -.
DR   SMR; A9R2J1; -.
DR   KEGG; ypg:YpAngola_A3155; -.
DR   PATRIC; fig|349746.12.peg.4214; -.
DR   OMA; IEMARIC; -.
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..218
FT                   /note="Flap endonuclease Xni"
FT                   /id="PRO_0000389452"
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   218 AA;  24134 MW;  07228E6573DD610C CRC64;
     MQIHLLIVDA LNLIRRIHAV QGSPCVKACQ HALQQLIQHS QPSHAVAVFD EDDRSDSWRH
     QCLPDYKAGR SPMPDNLQQE MPLIRQAFNE LGVACWHSPG NEADDLAATL VVKVAGAGHQ
     VTIVSTDKGY CQLLAPNIQI RDYFQKRWLD MPFVKQEFGV LPRQLPDYWG LAGISSSKIP
     GVAGVGAKTA TLLLQQADTC NERCNSDPHP TPEIRSRG