ID   END1_ECOLI              Reviewed;         235 AA.
AC   P25736; Q2M9P8;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   10-JUN-2026, entry version 152.
DE   RecName: Full=Endonuclease-1;
DE            EC=3.1.21.1;
DE   AltName: Full=Endonuclease I;
DE            Short=Endo I;
DE   Flags: Precursor;
GN   Name=endA; OrderedLocusNames=b2945, JW2912;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=7867949; DOI=10.1016/0378-1119(94)00835-g;
RA   Jekel M., Wackernagel W.;
RT   "The periplasmic endonuclease I of Escherichia coli has amino-acid sequence
RT   homology to the extracellular DNases of Vibrio cholerae and Aeromonas
RT   hydrophila.";
RL   Gene 154:55-59(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=4955462; DOI=10.1016/0006-291x(65)90434-1;
RA   Cordonnier C., Bernardi G.;
RT   "Localization of E. coli endonuclease I.";
RL   Biochem. Biophys. Res. Commun. 20:555-559(1965).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=14463751; DOI=10.1016/s0021-9258(18)60378-3;
RA   Lehman I.R., Roussos G.G., Pratt E.A.;
RT   "The deoxyribonuclease of Escherichia coli. II. Purification and properties
RT   of a ribonucleic acid-inhibitable endonuclease.";
RL   J. Biol. Chem. 237:819-828(1962).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=14463750; DOI=10.1016/s0021-9258(18)60379-5;
RA   Lehman I.R., Roussos G.G., Pratt E.A.;
RT   "The deoxyribonuclease of Escherichia coli. III. Studies on the nature of
RT   the inhibition of endonuclease by ribonucleic acid.";
RL   J. Biol. Chem. 237:829-833(1962).
RN   [7]
RP   GENE MAPPING.
RX   PubMed=8113204; DOI=10.1128/jb.176.5.1550-1551.1994;
RA   Jekel M., Wackernagel W.;
RT   "Location of the endA gene coding for endonuclease I on the physical map of
RT   the Escherichia coli K-12 chromosome.";
RL   J. Bacteriol. 176:1550-1551(1994).
CC   -!- FUNCTION: Has double-strand break activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-
CC         phosphooligonucleotide end-products.; EC=3.1.21.1;
CC   -!- ACTIVITY REGULATION: Inhibited by RNA.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:4955462}.
CC   -!- SIMILARITY: Belongs to the EndA/NucM nuclease family. {ECO:0000305}.
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DR   EMBL; X65169; CAA46287.1; -; Genomic_DNA.
DR   EMBL; U28377; AAA69112.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75982.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77008.1; -; Genomic_DNA.
DR   PIR; A38966; A38966.
DR   RefSeq; NP_417420.1; NC_000913.3.
DR   RefSeq; WP_000286500.1; NZ_CP009789.1.
DR   AlphaFoldDB; P25736; -.
DR   SMR; P25736; -.
DR   BioGRID; 4262350; 55.
DR   FunCoup; P25736; 106.
DR   STRING; 511145.b2945; -.
DR   PaxDb; 511145-b2945; -.
DR   EnsemblBacteria; AAC75982; AAC75982; b2945.
DR   GeneID; 93779052; -.
DR   GeneID; 949092; -.
DR   KEGG; ecj:JW2912; -.
DR   KEGG; eco:b2945; -.
DR   KEGG; ecoc:C3026_16120; -.
DR   PATRIC; fig|1411691.4.peg.3788; -.
DR   EchoBASE; EB1312; -.
DR   eggNOG; COG2356; Bacteria.
DR   HOGENOM; CLU_070541_0_0_6; -.
DR   InParanoid; P25736; -.
DR   OMA; LYMSKEY; -.
DR   OrthoDB; 9800417at2; -.
DR   PhylomeDB; P25736; -.
DR   BioCyc; EcoCyc:EG11336-MONOMER; -.
DR   BioCyc; MetaCyc:EG11336-MONOMER; -.
DR   PRO; PR:P25736; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004530; F:deoxyribonuclease I activity; IEA:UniProtKB-EC.
DR   GO; GO:0016888; F:DNA endonuclease activity, producing 5'-phosphomonoesters; IDA:EcoCyc.
DR   GO; GO:0004536; F:DNA nuclease activity; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IDA:EcoCyc.
DR   GO; GO:0006308; P:DNA catabolic process; IMP:EcoCyc.
DR   InterPro; IPR007346; Endonuclease-I.
DR   InterPro; IPR044925; His-Me_finger_sf.
DR   NCBIfam; NF011716; PRK15137.1; 1.
DR   PANTHER; PTHR33607; ENDONUCLEASE-1; 1.
DR   PANTHER; PTHR33607:SF2; ENDONUCLEASE-1; 1.
DR   Pfam; PF04231; Endonuclease_1; 1.
DR   SUPFAM; SSF54060; His-Me finger endonucleases; 1.
PE   1: Evidence at protein level;
KW   Endonuclease; Hydrolase; Nuclease; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..235
FT                   /note="Endonuclease-1"
FT                   /id="PRO_0000007827"
SQ   SEQUENCE   235 AA;  26709 MW;  EB0C355ADEF91EB3 CRC64;
     MYRYLSIAAV VLSAAFSGPA LAEGINSFSQ AKAAAVKVHA DAPGTFYCGC KINWQGKKGV
     VDLQSCGYQV RKNENRASRV EWEHVVPAWQ FGHQRQCWQD GGRKNCAKDP VYRKMESDMH
     NLQPSVGEVN GDRGNFMYSQ WNGGEGQYGQ CAMKVDFKEK AAEPPARARG AIARTYFYMR
     DQYNLTLSRQ QTQLFNAWNK MYPVTDWECE RDERIAKVQG NHNPYVQRAC QARKS
//