XNI_YERE8
ID XNI_YERE8 Reviewed; 251 AA.
AC A1JP96;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-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}; OrderedLocusNames=YE3297;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(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. {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; AM286415; CAL13327.1; -; Genomic_DNA.
DR RefSeq; WP_011816971.1; NC_008800.1.
DR RefSeq; YP_001007471.1; NC_008800.1.
DR AlphaFoldDB; A1JP96; -.
DR SMR; A1JP96; -.
DR STRING; 393305.YE3297; -.
DR EnsemblBacteria; CAL13327; CAL13327; YE3297.
DR KEGG; yen:YE3297; -.
DR PATRIC; fig|393305.7.peg.3507; -.
DR eggNOG; COG0258; Bacteria.
DR HOGENOM; CLU_004675_1_2_6; -.
DR OMA; WRVDLIP; -.
DR Proteomes; UP000000642; 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.
FT CHAIN 1..251
FT /note="Flap endonuclease Xni"
FT /id="PRO_0000297892"
FT DOMAIN 160..249
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT REGION 51..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 27937 MW; 2067390C40C20F88 CRC64;
MQIHLLIVDA LNLIRRIHAV QGSPSVNACQ HALQQLISHS QPTHAVAVFD EDDRSDSWRH
QSLPDYKAGR SPMSDNLQQE MPLIREAFNS LGVNCWSSPG NEADDLAATL AVKIGGAGHQ
VTIVSTDKGY CQLLAPNVQI RDYFQKRWLD MPFVKQEFGV LPHQLPDYWG LAGISSSKIP
GVAGIGAKTA ALLLQQASSL EQLYQELDSV PEKWRKKLQQ HQEMAFICKQ IATLKTDLPL
SGNLQQLRLN R
