ID   EX7S_POLSJ              Reviewed;          93 AA.
AC   Q12CR1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, 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=Bpro_1745;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE43681.1; -; Genomic_DNA.
DR   RefSeq; WP_011482680.1; NC_007948.1.
DR   AlphaFoldDB; Q12CR1; -.
DR   SMR; Q12CR1; -.
DR   STRING; 296591.Bpro_1745; -.
DR   EnsemblBacteria; ABE43681; ABE43681; Bpro_1745.
DR   KEGG; pol:Bpro_1745; -.
DR   eggNOG; COG1722; Bacteria.
DR   HOGENOM; CLU_145918_2_0_4; -.
DR   OMA; GDMLKPF; -.
DR   OrthoDB; 2057189at2; -.
DR   Proteomes; UP000001983; 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   SUPFAM; SSF116842; SSF116842; 1.
DR   TIGRFAMs; TIGR01280; xseB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..93
FT                   /note="Exodeoxyribonuclease 7 small subunit"
FT                   /id="PRO_1000205231"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   93 AA;  9745 MW;  EA3460A4F06E20F9 CRC64;
     MAKSSSSSSP SPAAASAATT SSAPPLPASY EAALQELEGL VAGLESGQLP LDQLLTGYQR
     GAQLLKFCRD KLEAVETQIK VLEGTELKPW VQE