ID   EX7S_LEGPA              Reviewed;          76 AA.
AC   Q5X2W0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=lpp2277;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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}.
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DR   EMBL; CR628336; CAH13430.1; -; Genomic_DNA.
DR   RefSeq; WP_011947173.1; NC_006368.1.
DR   AlphaFoldDB; Q5X2W0; -.
DR   SMR; Q5X2W0; -.
DR   KEGG; lpp:lpp2277; -.
DR   LegioList; lpp2277; -.
DR   HOGENOM; CLU_145918_3_2_6; -.
DR   OMA; PLNDYKG; -.
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.
FT   CHAIN           1..76
FT                   /note="Exodeoxyribonuclease 7 small subunit"
FT                   /id="PRO_0000206961"
SQ   SEQUENCE   76 AA;  8626 MW;  AA385AA196A161C1 CRC64;
     MSKGIHFEQS ITELEEIVRQ LEKGELTLEE SLKQFEKGIS LARRCQNALN QAEQKIETLT
     GTDSNIELDS DEQTSD