EX7S_GLUOX
ID EX7S_GLUOX Reviewed; 83 AA.
AC Q5FUB3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=GOX0250;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW60033.1; -; Genomic_DNA.
DR RefSeq; WP_011251836.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FUB3; -.
DR SMR; Q5FUB3; -.
DR STRING; 290633.GOX0250; -.
DR EnsemblBacteria; AAW60033; AAW60033; GOX0250.
DR GeneID; 56904517; -.
DR KEGG; gox:GOX0250; -.
DR eggNOG; COG1722; Bacteria.
DR HOGENOM; CLU_145918_0_3_5; -.
DR OMA; PLNDYKG; -.
DR Proteomes; UP000006375; 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..83
FT /note="Exodeoxyribonuclease 7 small subunit"
FT /id="PRO_0000206951"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 83 AA; 9006 MW; B08A555065CB1B61 CRC64;
MPEPIDAMSF EDALSELERI VRGLEGGQMK LEDAISAYER GAALRRHCDA KLGEAEMRVR
AIVQNDDGTT GTEPLADTGE SGR
