ID   EX7S_BURM7              Reviewed;          97 AA.
AC   A3MBD0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=BMA10247_A0362;
OS   Burkholderia mallei (strain NCTC 10247).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10247;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000547; ABO02519.1; -; Genomic_DNA.
DR   RefSeq; WP_004190549.1; NZ_CP007801.1.
DR   AlphaFoldDB; A3MBD0; -.
DR   SMR; A3MBD0; -.
DR   GeneID; 56598190; -.
DR   KEGG; bmaz:BM44_3369; -.
DR   KEGG; bmn:BMA10247_A0362; -.
DR   PATRIC; fig|320389.8.peg.3783; -.
DR   OMA; GDMLKPF; -.
DR   Proteomes; UP000002284; Chromosome II.
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   SUPFAM; SSF116842; SSF116842; 1.
DR   TIGRFAMs; TIGR01280; xseB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT   CHAIN           1..97
FT                   /note="Exodeoxyribonuclease 7 small subunit"
FT                   /id="PRO_1000019570"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   97 AA;  9967 MW;  010EDBAEC740BB4B CRC64;
     MAKTATPGAC ASDPGSGPLP ENYEMALAEL EALVARMEGG TLSLEDSLAA YRRGAALVAF
     CQQQLEKAEQ QVRVLDGASL KPLSAGTAAA DGEDDDL