ID A0A075R2C2_BRELA Unreviewed; 83 AA.
AC A0A075R2C2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Exodeoxyribonuclease 7 small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
DE EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00337};
DE AltName: Full=Exodeoxyribonuclease VII small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
DE Short=Exonuclease VII small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
GN Name=xseB {ECO:0000256|HAMAP-Rule:MF_00337};
GN ORFNames=BRLA_c016850 {ECO:0000313|EMBL:AIG26009.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG26009.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG26009.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG26009.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_00337};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00337}.
CC -!- SIMILARITY: Belongs to the XseB family. {ECO:0000256|ARBA:ARBA00009998,
CC ECO:0000256|HAMAP-Rule:MF_00337}.
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DR EMBL; CP007806; AIG26009.1; -; Genomic_DNA.
DR RefSeq; WP_003337884.1; NZ_CP007806.1.
DR AlphaFoldDB; A0A075R2C2; -.
DR STRING; 1042163.BRLA_c016850; -.
DR KEGG; blr:BRLA_c016850; -.
DR eggNOG; COG1722; Bacteria.
DR HOGENOM; CLU_145918_3_1_9; -.
DR Proteomes; UP000005850; 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; Exonuclease VII, small subunit; 1.
DR HAMAP; MF_00337; Exonuc_7_S; 1.
DR InterPro; IPR003761; Exonuc_VII_S.
DR InterPro; IPR037004; Exonuc_VII_ssu_sf.
DR NCBIfam; TIGR01280; xseB; 1.
DR PANTHER; PTHR34137; EXODEOXYRIBONUCLEASE 7 SMALL SUBUNIT; 1.
DR PANTHER; PTHR34137:SF1; EXODEOXYRIBONUCLEASE 7 SMALL SUBUNIT; 1.
DR Pfam; PF02609; Exonuc_VII_S; 1.
DR SUPFAM; SSF116842; XseB-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00337};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00337};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00337};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00337};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850}.
SQ SEQUENCE 83 AA; 9556 MW; AC2D2F1255E0E2BF CRC64;
MARKKAAQET ELLFEEAMQR LEEVVRQLEE GDVPLERAIE LYQEGIQLSR QCATKLDAIE
AKVIQLLDQD GSISERPFHV EED
//