ID   EX7L_SALSV              Reviewed;         449 AA.
AC   B4TR85;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=SeSA_A2746;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001127; ACF91638.1; -; Genomic_DNA.
DR   RefSeq; WP_000953174.1; NC_011094.1.
DR   AlphaFoldDB; B4TR85; -.
DR   SMR; B4TR85; -.
DR   EnsemblBacteria; ACF91638; ACF91638; SeSA_A2746.
DR   KEGG; sew:SeSA_A2746; -.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000001865; 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..449
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000122087"
SQ   SEQUENCE   449 AA;  50685 MW;  5A66BE97DAA91E77 CRC64;
     MLSSQTSSIF TVSRLNQTVR LLLEQEMGQV WISGEISNFT QPASGHWYFT LKDDTAQVRC
     AMFRNSNRRV TFRPQHGQQV LVRANITLYE PRGDYQIIAE SMQPAGEGLL QQKYEQLKAK
     LQAEGLFDQQ HKQQLPSPAH CVGVITSKTG AALHDILHVL KRRDPSLPVI IYPTAVQGDD
     APGQIVRAIE LANARGECDV LIVGRGGGSL EDLWSFNDER VARAIFASRI PVVSAVGHET
     DVTIADFVAD LRAPTPSAAA EIVSRNQQEL LRQIQSAQQR LGMAMDYYLA NRSRRFTQIF
     HRLQQQHPQL RLARQQTALE RLRQRMGFAL EARIKQATQR QQRVSQRLSQ QNPQPRIHRA
     QSRIQQLEYR LTENIRSRLS EQRERFGNAV THLEAVSPLA TLARGYTVST TTDGKVLKKI
     KQVKAGDIMT TRLEDGWLES EVKSVTPGT