EX7S_CLOB1
ID EX7S_CLOB1 Reviewed; 71 AA.
AC A7FUT9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=CLB_1821;
OS Clostridium botulinum (strain ATCC 19397 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441770;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19397 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000726; ABS33973.1; -; Genomic_DNA.
DR RefSeq; WP_011986443.1; NC_009697.1.
DR AlphaFoldDB; A7FUT9; -.
DR SMR; A7FUT9; -.
DR GeneID; 5186139; -.
DR KEGG; cba:CLB_1821; -.
DR HOGENOM; CLU_145918_3_2_9; -.
DR OMA; MNEYREY; -.
DR OrthoDB; 2057189at2; -.
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..71
FT /note="Exodeoxyribonuclease 7 small subunit"
FT /id="PRO_1000019576"
SQ SEQUENCE 71 AA; 8308 MW; 1ECAA2C1BC9FC359 CRC64;
MEKKKESFEN MLEKLETIVD SMDNGEITLE DSMKSYEEGI KLCNKLYKVL KDAEGKIKIL
ENNKEEDFEN S