RECE_ECOLI
ID RECE_ECOLI Reviewed; 866 AA.
AC P15032; P76848; P77807;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Exodeoxyribonuclease 8;
DE EC=3.1.11.-;
DE AltName: Full=Exodeoxyribonuclease VIII;
DE Short=EXO VIII;
GN Name=recE; OrderedLocusNames=b1350, JW1344;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-661.
RC STRAIN=K12;
RX PubMed=2649487; DOI=10.1128/jb.171.4.2101-2109.1989;
RA Chu C.C., Templin A., Clark A.J.;
RT "Suppression of a frameshift mutation in the recE gene of Escherichia coli
RT K-12 occurs by gene fusion.";
RL J. Bacteriol. 171:2101-2109(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 295-346.
RC STRAIN=K12;
RX PubMed=2199308; DOI=10.1093/genetics/125.2.261;
RA Mahajan S.K., Chu C.C., Willis D.K., Templin A., Clark A.J.;
RT "Physical analysis of spontaneous and mutagen-induced mutants of
RT Escherichia coli K-12 expressing DNA exonuclease VIII activity.";
RL Genetics 125:261-273(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 660-866.
RC STRAIN=K12;
RX PubMed=8244937; DOI=10.1128/jb.175.23.7673-7682.1993;
RA Clark A.J., Sharma V., Brenowitz S., Chu C.C., Sandler S.J., Satin L.,
RA Templin A., Berger I., Cohen A.;
RT "Genetic and molecular analyses of the C-terminal region of the recE gene
RT from the Rac prophage of Escherichia coli K-12 reveal the recT gene.";
RL J. Bacteriol. 175:7673-7682(1993).
RN [7]
RP INDUCTION BY 2,4,6-TRINITROTOLUENE, AND BIOTECHNOLOGY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=25561288; DOI=10.1007/s12013-014-0481-8;
RA Tan J., Kan N., Wang W., Ling J., Qu G., Jin J., Shao Y., Liu G., Chen H.;
RT "Construction of 2,4,6-trinitrotoluene biosensors with novel sensing
RT elements from Escherichia coli K-12 MG1655.";
RL Cell Biochem. Biophys. 72:417-428(2015).
CC -!- FUNCTION: Is involved in the RecE pathway of recombination. Catalyzes
CC the degradation of double-stranded DNA. Acts progressively in a 5' to
CC 3' direction, releasing 5'-phosphomononucleotides. Has a strong
CC preference for linear duplex substrate DNA and appears to be unable to
CC initiate degradation from single-stranded breaks in DNA.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P15032; P15032: recE; NbExp=2; IntAct=EBI-553304, EBI-553304;
CC -!- INDUCTION: Transcription is increased specifically in response to
CC 2,4,6-trinitrotoluene (TNT) and its indicator compounds 1,3-DNB, 2,4-
CC DNT, and 2,6-DNT. {ECO:0000269|PubMed:25561288}.
CC -!- BIOTECHNOLOGY: Has been used to construct a 2,4,6-trinitrotoluene (TNT)
CC biosensor strain. {ECO:0000269|PubMed:25561288}.
CC -!- MISCELLANEOUS: Encoded in the Rac prophage. {ECO:0000305}.
CC -!- CAUTION: The protein sequences in X55956 are all from mutants in which
CC fusions to an internal fragment of recE have occurred.
CC {ECO:0000305|PubMed:2199308}.
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DR EMBL; U00096; AAC74432.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14950.1; -; Genomic_DNA.
DR EMBL; M24905; AAA03212.1; -; Unassigned_DNA.
DR EMBL; X55956; CAA39419.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X55956; CAA39420.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X55956; CAA39421.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X55956; CAA39422.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X55956; CAA39423.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L23927; AAA16178.1; -; Unassigned_DNA.
DR PIR; A64885; NCECX8.
DR RefSeq; NP_415866.1; NC_000913.3.
DR RefSeq; WP_000105143.1; NZ_CP047127.1.
DR PDB; 3H4R; X-ray; 2.80 A; A=606-866.
DR PDBsum; 3H4R; -.
DR AlphaFoldDB; P15032; -.
DR SMR; P15032; -.
DR BioGRID; 4260163; 103.
DR DIP; DIP-10652N; -.
DR IntAct; P15032; 11.
DR STRING; 511145.b1350; -.
DR PaxDb; P15032; -.
DR PRIDE; P15032; -.
DR EnsemblBacteria; AAC74432; AAC74432; b1350.
DR EnsemblBacteria; BAA14950; BAA14950; BAA14950.
DR GeneID; 945918; -.
DR KEGG; ecj:JW1344; -.
DR KEGG; eco:b1350; -.
DR PATRIC; fig|1411691.4.peg.927; -.
DR EchoBASE; EB0820; -.
DR eggNOG; COG0847; Bacteria.
DR OMA; WKFTSAN; -.
DR PhylomeDB; P15032; -.
DR BioCyc; EcoCyc:EG10827-MON; -.
DR BioCyc; MetaCyc:EG10827-MON; -.
DR EvolutionaryTrace; P15032; -.
DR PRO; PR:P15032; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051908; F:double-stranded DNA 5'-3' exodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR010584; ExoDNase_VIII.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR024432; Put_RecE_PDDEXK-like_dom.
DR Pfam; PF12684; DUF3799; 1.
DR Pfam; PF06630; Exonuc_VIII; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..866
FT /note="Exodeoxyribonuclease 8"
FT /id="PRO_0000097227"
FT REGION 368..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 366
FT /note="A -> G (in Ref. 4; AAA03212)"
FT /evidence="ECO:0000305"
FT CONFLICT 691..692
FT /note="ST -> TA (in Ref. 6; AAA16178)"
FT /evidence="ECO:0000305"
FT HELIX 616..624
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 626..632
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 647..655
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 658..661
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 704..712
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 716..722
FT /evidence="ECO:0007829|PDB:3H4R"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:3H4R"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:3H4R"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:3H4R"
FT TURN 737..739
FT /evidence="ECO:0007829|PDB:3H4R"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:3H4R"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:3H4R"
FT STRAND 756..764
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 766..772
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 773..775
FT /evidence="ECO:0007829|PDB:3H4R"
FT TURN 776..779
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 780..793
FT /evidence="ECO:0007829|PDB:3H4R"
FT STRAND 798..807
FT /evidence="ECO:0007829|PDB:3H4R"
FT STRAND 815..819
FT /evidence="ECO:0007829|PDB:3H4R"
FT HELIX 822..844
FT /evidence="ECO:0007829|PDB:3H4R"
SQ SEQUENCE 866 AA; 96368 MW; 6133E2FDDB12A538 CRC64;
MSTKPLFLLR KAKKSSGEPD VVLWASNDFE STCATLDYLI VKSGKKLSSY FKAVATNFPV
VNDLPAEGEI DFTWSERYQL SKDSMTWELK PGAAPDNAHY QGNTNVNGED MTEIEENMLL
PISGQELPIR WLAQHGSEKP VTHVSRDGLQ ALHIARAEEL PAVTALAVSH KTSLLDPLEI
RELHKLVRDT DKVFPNPGNS NLGLITAFFE AYLNADYTDR GLLTKEWMKG NRVSHITRTA
SGANAGGGNL TDRGEGFVHD LTSLARDVAT GVLARSMDLD IYNLHPAHAK RIEEIIAENK
PPFSVFRDKF ITMPGGLDYS RAIVVASVKE APIGIEVIPA HVTEYLNKVL TETDHANPDP
EIVDIACGRS SAPMPQRVTE EGKQDDEEKP QPSGTTAVEQ GEAETMEPDA TEHHQDTQPL
DAQSQVNSVD AKYQELRAEL HEARKNIPSK NPVDDDKLLA ASRGEFVDGI SDPNDPKWVK
GIQTRDCVYQ NQPETEKTSP DMNQPEPVVQ QEPEIACNAC GQTGGDNCPD CGAVMGDATY
QETFDEESQV EAKENDPEEM EGAEHPHNEN AGSDPHRDCS DETGEVADPV IVEDIEPGIY
YGISNENYHA GPGISKSQLD DIADTPALYL WRKNAPVDTT KTKTLDLGTA FHCRVLEPEE
FSNRFIVAPE FNRRTNAGKE EEKAFLMECA STGKTVITAE EGRKIELMYQ SVMALPLGQW
LVESAGHAES SIYWEDPETG ILCRCRPDKI IPEFHWIMDV KTTADIQRFK TAYYDYRYHV
QDAFYSDGYE AQFGVQPTFV FLVASTTIEC GRYPVEIFMM GEEAKLAGQQ EYHRNLRTLS
DCLNTDEWPA IKTLSLPRWA KEYAND
