END1_ECOLI
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 03-AUG-2022, entry version 138.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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;
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;
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_STEB01000001.1.
DR AlphaFoldDB; P25736; -.
DR SMR; P25736; -.
DR BioGRID; 4262350; 55.
DR STRING; 511145.b2945; -.
DR PaxDb; P25736; -.
DR PRIDE; P25736; -.
DR EnsemblBacteria; AAC75982; AAC75982; b2945.
DR EnsemblBacteria; BAE77008; BAE77008; BAE77008.
DR GeneID; 66673174; -.
DR GeneID; 949092; -.
DR KEGG; ecj:JW2912; -.
DR KEGG; eco:b2945; -.
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; ADQYGQC; -.
DR PhylomeDB; P25736; -.
DR BioCyc; EcoCyc:EG11336-MON; -.
DR BioCyc; MetaCyc:EG11336-MON; -.
DR PRO; PR:P25736; -.
DR Proteomes; UP000000318; Chromosome.
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:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IDA:EcoCyc.
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 PANTHER; PTHR33607; PTHR33607; 1.
DR Pfam; PF04231; Endonuclease_1; 1.
DR SUPFAM; SSF54060; SSF54060; 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
