ID   EX7L_ECOHS              Reviewed;         456 AA.
AC   A8A315;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
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}; OrderedLocusNames=EcHS_A2660;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(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; CP000802; ABV06919.1; -; Genomic_DNA.
DR   RefSeq; WP_000937920.1; NC_009800.1.
DR   AlphaFoldDB; A8A315; -.
DR   KEGG; ecx:EcHS_A2660; -.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000001123; Chromosome.
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_1000060027"
SQ   SEQUENCE   456 AA;  51784 MW;  258B1E1F82C0BDE5 CRC64;
     MLPSQSPAIF TVSRLNQTVR LLLEHEMGQV WISGEISNFT QPASGHWYFT LKDDTAQVRC
     AMFRNSNRRV TFRPQHGQQV LVRANITLYE PRGDYQIIVE SMQPAGEGLL QQKYEQLKAK
     LQAEGLFDQQ YKKPLPSPAH CVGVITSKTG AALHDILHVL KRRDPSLPVI IYPTAVQGDD
     APGQIVRAIE LANQRNECDV LIVGRGGGSL EDLWSFNDER VARAIFASRI PVVSAVGHET
     DVTIADFVAD LRAPTPSAAA EVVSRNQQEL LRQVQSARQR LEMAMDYYLA NRTRRFTQIH
     HRLQQQHPQL RLARQQTMLE RLKKRMSFAL ENQLKRAGQQ QQRLTQRLNQ QNPQPKIHRA
     QTRIQQLEYR LAEILRAQLS ATRERFGNAV THLEAVSPLS TLARGYSVTT ATDGNVLKKV
     KQVKAGEMLT TRLEDGWIES EVKNIQPVKK SRKKVH