ID   XNI_SHEPA               Reviewed;         256 AA.
AC   A8H6V6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Spea_2976;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) 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; CP000851; ABV88293.1; -; Genomic_DNA.
DR   RefSeq; WP_012156197.1; NC_009901.1.
DR   AlphaFoldDB; A8H6V6; -.
DR   SMR; A8H6V6; -.
DR   STRING; 398579.Spea_2976; -.
DR   EnsemblBacteria; ABV88293; ABV88293; Spea_2976.
DR   KEGG; spl:Spea_2976; -.
DR   eggNOG; COG0258; Bacteria.
DR   HOGENOM; CLU_004675_1_2_6; -.
DR   OMA; WRVDLIP; -.
DR   Proteomes; UP000002608; Chromosome.
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; Reference proteome.
FT   CHAIN           1..256
FT                   /note="Flap endonuclease Xni"
FT                   /id="PRO_1000085478"
FT   DOMAIN          163..256
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   REGION          185..190
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         173
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         181
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         183
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT   BINDING         186
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
SQ   SEQUENCE   256 AA;  28597 MW;  BA21A6E302BF0818 CRC64;
     MNKLLIIDGM NLVRRIHAAQ PNESDITGLK ERVHGACRKL LKYHIPTHAA IVWDGDAISW
     RKTLFPDYKK GRKPMPEALA NGLNDIKAYL AEHHIHSVDA DSEADDVIAT LATKLVNIDG
     EAIIVSTDKG FSQLNHPKIK LWDHFNQTYL TIEEMEKKLG IERSQLIDYL ALAGDSGNKI
     PGVPGIGPKS AVELLRIYRS LASIYNSIDK VGAKQAKKLE AGKQMARLSY KLVQLKTDMP
     LSVNLKQFRI KKPDSE