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Database: UniProt
Entry: G7LNV6_9GAMM
LinkDB: G7LNV6_9GAMM
Original site: G7LNV6_9GAMM 
ID   G7LNV6_9GAMM            Unreviewed;        80 AA.
AC   G7LNV6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=BrE312_3382 {ECO:0000313|EMBL:EHD22747.1};
OS   Brenneria sp. EniD312.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Brenneria.
OX   NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD22747.1};
RN   [1] {ECO:0000313|EMBL:EHD22747.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EniD312 {ECO:0000313|EMBL:EHD22747.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA   Glasner J., Perna N., Woyke T.;
RT   "Complete sequence of Brenneria sp. EniD312.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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; CM001230; EHD22747.1; -; Genomic_DNA.
DR   RefSeq; WP_009114045.1; NZ_CM001230.1.
DR   AlphaFoldDB; G7LNV6; -.
DR   STRING; 598467.BrE312_3382; -.
DR   eggNOG; COG1722; Bacteria.
DR   HOGENOM; CLU_145918_3_3_6; -.
DR   Proteomes; UP000002759; 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   PIRSF; PIRSF006488; 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}.
SQ   SEQUENCE   80 AA;  8970 MW;  32FACAF219766F49 CRC64;
     MPKKTEPPVS FESSLSELEK IVARLESGEL PLEEALNEFE HGVRLARQGQ QKLQQAEQRV
     QILLSDEPDA PLSPFTPDSE
//
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