XNI_CROS8
ID XNI_CROS8 Reviewed; 251 AA.
AC A7MR03;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=ESA_00506;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(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. {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; CP000783; ABU75798.1; -; Genomic_DNA.
DR RefSeq; WP_012123906.1; NC_009778.1.
DR AlphaFoldDB; A7MR03; -.
DR SMR; A7MR03; -.
DR EnsemblBacteria; ABU75798; ABU75798; ESA_00506.
DR KEGG; esa:ESA_00506; -.
DR PATRIC; fig|290339.8.peg.456; -.
DR HOGENOM; CLU_004675_1_2_6; -.
DR OMA; WRVDLIP; -.
DR OrthoDB; 1220182at2; -.
DR Proteomes; UP000000260; 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_1000065880"
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; 27835 MW; 8F52B689309E6F87 CRC64;
MPVHLLIVDA LNLIRRIHAV QGTPCVDTCL HALEQLIGNS QPTHAVAVFD DEARAQGWRH
QLLPDYKAGR PPMPDDLHQE MPALRDAFTR RGVPCWHVEG NEADDLAATL AVKVAAAGHE
ATIVSTDKGY CQLLRPEIRI RDYFQKRWLD APFIESEFGV SPGQLADFWG LAGISSSKIP
GVPGIGPKSA TQLINDFGTL EALYERLDDV PDKWRKKLEA HRESAFVCRA VATLKTDLQL
DGNLQQLRLH G
