ID   EX7S_CLOPE              Reviewed;          75 AA.
AC   Q8XJD9;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Exodeoxyribonuclease 7 small subunit {ECO:0000255|HAMAP-Rule:MF_00337};
DE            EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00337};
DE   AltName: Full=Exodeoxyribonuclease VII small subunit {ECO:0000255|HAMAP-Rule:MF_00337};
DE            Short=Exonuclease VII small subunit {ECO:0000255|HAMAP-Rule:MF_00337};
GN   Name=xseB {ECO:0000255|HAMAP-Rule:MF_00337}; OrderedLocusNames=CPE1821;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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_00337}.
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_00337};
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00337}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00337}.
CC   -!- SIMILARITY: Belongs to the XseB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00337, ECO:0000305}.
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DR   EMBL; BA000016; BAB81527.1; -; Genomic_DNA.
DR   RefSeq; WP_003451121.1; NC_003366.1.
DR   AlphaFoldDB; Q8XJD9; -.
DR   SMR; Q8XJD9; -.
DR   STRING; 195102.gene:10491085; -.
DR   EnsemblBacteria; BAB81527; BAB81527; BAB81527.
DR   GeneID; 29570821; -.
DR   KEGG; cpe:CPE1821; -.
DR   HOGENOM; CLU_145918_3_2_9; -.
DR   OMA; MNEYREY; -.
DR   Proteomes; UP000000818; 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:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.1040; -; 1.
DR   HAMAP; MF_00337; Exonuc_7_S; 1.
DR   InterPro; IPR003761; Exonuc_VII_S.
DR   InterPro; IPR037004; Exonuc_VII_ssu_sf.
DR   PANTHER; PTHR34137; PTHR34137; 1.
DR   Pfam; PF02609; Exonuc_VII_S; 1.
DR   PIRSF; PIRSF006488; Exonuc_VII_S; 1.
DR   SUPFAM; SSF116842; SSF116842; 1.
DR   TIGRFAMs; TIGR01280; xseB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..75
FT                   /note="Exodeoxyribonuclease 7 small subunit"
FT                   /id="PRO_0000206940"
SQ   SEQUENCE   75 AA;  8669 MW;  7EE63B607AF6F31F CRC64;
     MARKETNYES MVSELNEIVK QLENGDLTLE ESIKSYENGV KIVNKLYKKL STLEGKIKVV
     EDEKEEDFGG YSNEY