XNI_SHIDS
ID XNI_SHIDS Reviewed; 251 AA.
AC Q32CC0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=SDY_3015;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB63035.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000034; ABB63035.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000268232.1; NC_007606.1.
DR RefSeq; YP_404526.1; NC_007606.1.
DR AlphaFoldDB; Q32CC0; -.
DR SMR; Q32CC0; -.
DR STRING; 300267.SDY_3015; -.
DR EnsemblBacteria; ABB63035; ABB63035; SDY_3015.
DR KEGG; sdy:SDY_3015; -.
DR PATRIC; fig|300267.13.peg.3619; -.
DR HOGENOM; CLU_004675_1_2_6; -.
DR Proteomes; UP000002716; 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..251
FT /note="Flap endonuclease Xni"
FT /id="PRO_0000297883"
FT DOMAIN 160..249
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; 28166 MW; 937A2CDCC58B03A5 CRC64;
MAVHLLIVDA LNLIRRIHAV QGSPCVETCQ HALDQLIMHS QPTHAVAVFD DENRSSGWRH
QRLPDYKAGR PPMPEELHDE MPALRAAFEQ RGVPCWSTSG NEADDLAATL AVKVTQAGHQ
ATIVSTDKGY CQLLSPTLRI RDYFQKRWLD APFIDKEFGV QPQQLPDYWG LAGISSSKVP
GVAGIGPKSA TQLLVEFQSL EGIYENLDAV AEKWRKKLET HKEMAFLCRD IARLQTDLHI
DGNLQQLRLV R
