ID   EXOX_ECOLI              Reviewed;         220 AA.
AC   P0AEK0; P76281; Q2MB09;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Exodeoxyribonuclease 10;
DE            EC=3.1.11.-;
DE   AltName: Full=Exodeoxyribonuclease X;
DE            Short=Exo X;
DE            Short=Exonuclease X;
GN   Name=exoX; Synonyms=yobC; OrderedLocusNames=b1844, JW1833;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=10514496; DOI=10.1074/jbc.274.42.30094;
RA   Viswanathan M., Lovett S.T.;
RT   "Exonuclease X of Escherichia coli. A novel 3'-5' DNase and DnaQ
RT   superfamily member involved in DNA repair.";
RL   J. Biol. Chem. 274:30094-30100(1999).
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).
CC   -!- FUNCTION: Capable of degrading both single-strand and double-strand DNA
CC       with 3' to 5' polarity. Has higher affinity for ssDNA ends than for
CC       dsDNA.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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DR   EMBL; AF194116; AAF04847.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74914.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76547.1; -; Genomic_DNA.
DR   PIR; D64946; D64946.
DR   RefSeq; NP_416358.1; NC_000913.3.
DR   RefSeq; WP_000944256.1; NZ_STEB01000009.1.
DR   PDB; 4FZX; X-ray; 2.30 A; C/D=1-167.
DR   PDB; 4FZY; X-ray; 2.50 A; A/B=1-167.
DR   PDB; 4FZZ; X-ray; 2.80 A; A/B=1-167.
DR   PDBsum; 4FZX; -.
DR   PDBsum; 4FZY; -.
DR   PDBsum; 4FZZ; -.
DR   AlphaFoldDB; P0AEK0; -.
DR   SMR; P0AEK0; -.
DR   BioGRID; 4260363; 106.
DR   STRING; 511145.b1844; -.
DR   jPOST; P0AEK0; -.
DR   PaxDb; 511145-b1844; -.
DR   EnsemblBacteria; AAC74914; AAC74914; b1844.
DR   GeneID; 75202671; -.
DR   GeneID; 946361; -.
DR   KEGG; ecj:JW1833; -.
DR   KEGG; eco:b1844; -.
DR   PATRIC; fig|511145.12.peg.1922; -.
DR   EchoBASE; EB3785; -.
DR   eggNOG; COG0847; Bacteria.
DR   HOGENOM; CLU_047806_8_2_6; -.
DR   InParanoid; P0AEK0; -.
DR   OMA; SPYYVAH; -.
DR   OrthoDB; 7822240at2; -.
DR   PhylomeDB; P0AEK0; -.
DR   BioCyc; EcoCyc:G7016-MONOMER; -.
DR   PRO; PR:P0AEK0; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:EcoCyc.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; IDA:EcoCyc.
DR   CDD; cd06127; DEDDh; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR046768; ExoX-like_C.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR   PANTHER; PTHR30231:SF4; PROTEIN NEN2; 1.
DR   Pfam; PF20600; ExoX-like_C; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA repair; Exonuclease; Hydrolase; Magnesium;
KW   Nuclease; Reference proteome.
FT   CHAIN           1..220
FT                   /note="Exodeoxyribonuclease 10"
FT                   /id="PRO_0000087136"
FT   STRAND          2..11
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   STRAND          16..25
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           45..51
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           55..58
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           68..71
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           82..88
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           99..106
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           114..120
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           136..154
FT                   /evidence="ECO:0007829|PDB:4FZX"
FT   HELIX           158..165
FT                   /evidence="ECO:0007829|PDB:4FZX"
SQ   SEQUENCE   220 AA;  25133 MW;  A1863A22C8C57A6F CRC64;
     MLRIIDTETC GLQGGIVEIA SVDVIDGKIV NPMSHLVRPD RPISPQAMAI HRITEAMVAD
     KPWIEDVIPH YYGSEWYVAH NASFDRRVLP EMPGEWICTM KLARRLWPGI KYSNMALYKT
     RKLNVQTPPG LHHHRALYDC YITAALLIDI MNTSGWTAEQ MADITGRPSL MTTFTFGKYR
     GKAVSDVAER DPGYLRWLFN NLDSMSPELR LTLKHYLENT
//