EX7L_ECODH
ID EX7L_ECODH Reviewed; 456 AA.
AC B1XAY4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378};
GN OrderedLocusNames=ECDH10B_2675;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-
CC insoluble oligonucleotides, which are then degraded further into small
CC acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00378};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC Rule:MF_00378}.
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DR EMBL; CP000948; ACB03661.1; -; Genomic_DNA.
DR RefSeq; WP_000937912.1; NC_010473.1.
DR AlphaFoldDB; B1XAY4; -.
DR KEGG; ecd:ECDH10B_2675; -.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR BioCyc; ECOL316385:ECDH10B_RS13605-MON; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro.
DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04489; ExoVII_LU_OBF; 1.
DR HAMAP; MF_00378; Exonuc_7_L; 1.
DR InterPro; IPR003753; Exonuc_VII_L.
DR InterPro; IPR020579; Exonuc_VII_lsu_C.
DR InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR PANTHER; PTHR30008; PTHR30008; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
DR TIGRFAMs; TIGR00237; xseA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT CHAIN 1..456
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122057"
SQ SEQUENCE 456 AA; 51832 MW; A5E5B138C54A7D27 CRC64;
MLPSQSPAIF TVSRLNQTVR LLLEHEMGQV WISGEISNFT QPASGHWYFT LKDDTAQVRC
AMFRNSNRRV TFRPQHGQQV LVRANITLYE PRGDYQIIVE SMQPAGEGLL QQKYEQLKAK
LQAEGLFDQQ YKKPLPSPAH CVGVITSKTG AALHDILHVL KRRDPSLPVI IYPAAVQGDD
APGQIVRAIE LANQRNECDV LIVGRGGGSL EDLWSFNDER VARAIFTSRI PVVSAVGHET
DVTIADFVAD LRAPTPSAAA EVVSRNQQEL LRQVQSTRQR LEMAMDYYLA NRTRRFTQIH
HRLQQQHPQL RLARQQTMLE RLQKRMSFAL ENQLKRTGQQ QQRLTQRLNQ QNPQPKIHRA
QTRIQQLEYR LAETLRAQLS ATRERFGNAV THLEAVSPLS TLARGYSVTT ATDGNVLKKV
KQVKAGEMLT TRLEDGWIES EVKNIQPVKK SRKKVH
