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Database: UniProt
Entry: A0A2M9HPJ7_9BIFI
LinkDB: A0A2M9HPJ7_9BIFI
Original site: A0A2M9HPJ7_9BIFI 
ID   A0A2M9HPJ7_9BIFI        Unreviewed;       102 AA.
AC   A0A2M9HPJ7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=CUU80_07180 {ECO:0000313|EMBL:PJM78748.1};
OS   Bifidobacterium scaligerum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=2052656 {ECO:0000313|EMBL:PJM78748.1, ECO:0000313|Proteomes:UP000228755};
RN   [1] {ECO:0000313|EMBL:PJM78748.1, ECO:0000313|Proteomes:UP000228755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRED {ECO:0000313|Proteomes:UP000228755};
RA   Mattarelli P., Modesto M., Bonetti A., Puglisi E., Morelli L.;
RT   "Draft genome sequences of strains TRE 1, TRE D, TRE H and TRI 7, isolated
RT   from tamarins, belonging to four potential novel Bifidobacterium species.";
RL   Submitted (NOV-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJM78748.1}.
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DR   EMBL; PGLQ01000004; PJM78748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9HPJ7; -.
DR   OrthoDB; 5244334at2; -.
DR   Proteomes; UP000228755; Unassembled WGS sequence.
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:UP000228755}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   102 AA;  10986 MW;  F57F526CCC8CB15D CRC64;
     MTNTNTETNA AATAPASSLT DKERELIAQM PYEEARDKLI QAVQALETGG LNLDQSMRQW
     EIGEALAKRA QGLLNEVRAK LDQAQADQAA NQATAGTQSN LD
//
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