ID   EX7L_CLOBB              Reviewed;         399 AA.
AC   B2TRM8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=CLL_A2404;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001056; ACD24147.1; -; Genomic_DNA.
DR   RefSeq; WP_012424923.1; NC_018648.1.
DR   AlphaFoldDB; B2TRM8; -.
DR   SMR; B2TRM8; -.
DR   EnsemblBacteria; ACD24147; ACD24147; CLL_A2404.
DR   KEGG; cbk:CLL_A2404; -.
DR   PATRIC; fig|935198.13.peg.2362; -.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000001195; 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; 2.
DR   Pfam; PF02601; Exonuc_VII_L; 2.
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..399
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000122049"
SQ   SEQUENCE   399 AA;  45095 MW;  4CC82ADD4668CA32 CRC64;
     MKIKTLTVSD LTNYIKKVID NDFILNNLSV KGEISNLKFH SSGHIYFSLK DNNSKVNCVM
     FKSKASLLNI ALEDGMEVMV KGRASIYTAT GSFQLYCDEI KKEGQGELFI KFEALKEKLS
     KSGYFDEKYK KNIPMYAKRI GIVTSSTGAV IRDIINVTKR RNSLVDIILY PAKVQGDNAY
     KEIIAGIEYF NKKKNIDIII VGRGGGSIEE LWNFNEEELA KVIFNSKLPI ISAVGHEVDF
     TISDFVSDVR AATPSQAAEI AVPLLSDINT RIYEISKSLD YEIQKKLKDC KSRLESNERI
     LKLHSPISKI VNSYLEIDKL KDRLYFAIDI KIKREKQKIE SLNNLLSANN PIKVLNKGYA
     IIEDENNNII KEISQLNEEK EISVSLSDGN IKGNFIPIK