ID   XNI_YERPY               Reviewed;         251 AA.
AC   B1JQE9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Flap endonuclease Xni {ECO:0000255|HAMAP-Rule:MF_01192};
DE            Short=FEN {ECO:0000255|HAMAP-Rule:MF_01192};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01192};
GN   Name=xni {ECO:0000255|HAMAP-Rule:MF_01192};
GN   Synonyms=ygdG {ECO:0000255|HAMAP-Rule:MF_01192};
GN   OrderedLocusNames=YPK_1055;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01192}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01192};
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:0000255|HAMAP-Rule:MF_01192};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01192};
CC       Note=Binds 1 K(+) per subunit. The potassium ion strongly increases the
CC       affinity for DNA. {ECO:0000255|HAMAP-Rule:MF_01192};
CC   -!- SIMILARITY: Belongs to the Xni family. {ECO:0000255|HAMAP-
CC       Rule:MF_01192}.
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DR   EMBL; CP000950; ACA67356.1; -; Genomic_DNA.
DR   RefSeq; WP_011192868.1; NZ_CP009792.1.
DR   AlphaFoldDB; B1JQE9; -.
DR   SMR; B1JQE9; -.
DR   EnsemblBacteria; ACA67356; ACA67356; YPK_1055.
DR   GeneID; 66844556; -.
DR   KEGG; ypy:YPK_1055; -.
DR   PATRIC; fig|502800.11.peg.1687; -.
DR   OMA; WRVDLIP; -.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   HAMAP; MF_01192; Xni; 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   InterPro; IPR022895; Xni.
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..251
FT                   /note="Flap endonuclease Xni"
FT                   /id="PRO_1000138399"
FT   DOMAIN          160..250
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   REGION          184..189
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         171
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         172
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         180
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         182
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         185
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
SQ   SEQUENCE   251 AA;  28146 MW;  2B82720197B9EFF2 CRC64;
     MQIHLLIVDA LNLIRRIHAV QGSPCVKACQ HALQQLIQHS QPSHAVAVFD EDDRSDSWRH
     QCLPDYKAGR SPMPDNLQQE MPLIRQAFNE LGVACWHSPG NEADDLAATL VVKVAGAGHQ
     VTIVSTDKGY CQLLAPNVQI RDYFQKRWLD MPFVKQEFGV LPRQLPDYWG LAGISSSKIP
     GVAGVGAKTA TLLLQQADTL EVLYQNLESI PEKWRKKLQQ HQQMAFTCKQ IATLKTDLLL
     SGNLQQLRLK K