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Database: UniProt
Entry: A0A1P8WY60_9SPHN
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Original site: A0A1P8WY60_9SPHN 
ID   A0A1P8WY60_9SPHN        Unreviewed;        87 AA.
AC   A0A1P8WY60;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=BWQ93_11020 {ECO:0000313|EMBL:APZ98964.1};
OS   Sphingopyxis sp. QXT-31.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1357916 {ECO:0000313|EMBL:APZ98964.1, ECO:0000313|Proteomes:UP000188055};
RN   [1] {ECO:0000313|EMBL:APZ98964.1, ECO:0000313|Proteomes:UP000188055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QXT-31 {ECO:0000313|EMBL:APZ98964.1,
RC   ECO:0000313|Proteomes:UP000188055};
RA   Liang J.S.;
RT   "Microbe-microbe interactions indirectly alter the fate of arsenic in
RT   presence of MnII.";
RL   Submitted (JAN-2017) 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; CP019449; APZ98964.1; -; Genomic_DNA.
DR   RefSeq; WP_077030590.1; NZ_CP019449.1.
DR   AlphaFoldDB; A0A1P8WY60; -.
DR   STRING; 1357916.BWQ93_11020; -.
DR   KEGG; sphq:BWQ93_11020; -.
DR   OrthoDB; 9808145at2; -.
DR   Proteomes; UP000188055; 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:UP000188055}.
SQ   SEQUENCE   87 AA;  9012 MW;  12420F02C2D43FC4 CRC64;
     MTDTPDSPAA PAISALSFEA AMSELETIVR RLESGDVSLE ESVALYERGH ALRGHCEARL
     AAAQARIEQV SLGADGRAAG TAPFGEG
//
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