EX7L_STAA8
ID EX7L_STAA8 Reviewed; 445 AA.
AC Q2FY46;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378};
GN OrderedLocusNames=SAOUHSC_01620;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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_00378}.
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_00378};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC Rule:MF_00378}.
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DR EMBL; CP000253; ABD30698.1; -; Genomic_DNA.
DR RefSeq; WP_001286928.1; NZ_LS483365.1.
DR RefSeq; YP_500134.1; NC_007795.1.
DR AlphaFoldDB; Q2FY46; -.
DR SMR; Q2FY46; -.
DR STRING; 1280.SAXN108_1547; -.
DR EnsemblBacteria; ABD30698; ABD30698; SAOUHSC_01620.
DR GeneID; 3919958; -.
DR KEGG; sao:SAOUHSC_01620; -.
DR PATRIC; fig|93061.5.peg.1474; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
DR PRO; PR:Q2FY46; -.
DR Proteomes; UP000008816; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04489; ExoVII_LU_OBF; 1.
DR HAMAP; MF_00378; Exonuc_7_L; 1.
DR InterPro; IPR003753; Exonuc_VII_L.
DR InterPro; IPR020579; Exonuc_VII_lsu_C.
DR InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR PANTHER; PTHR30008; PTHR30008; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
DR TIGRFAMs; TIGR00237; xseA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..445
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000273696"
SQ SEQUENCE 445 AA; 50894 MW; 172C12F9B18EA4EF CRC64;
MSDYLSVSAL TKYIKYKFDQ DPHLQSVLIK GELSNFKKHS SGHLYFNVKD KESVISAMMF
KGSASKLNFE PKEGDEVLLE ARVSVFERRG NYQIYVNKMQ LDGIGNLYQK LEALKKKLTE
EGCFDKANKK SIPKFPKKIA VLTASTGAAI RDIHSTINSR FPLAEQIQIS TLVQGEKAKD
DIIEKIEYAD SLGVDTIIVG RGGGSIEDLW NFNEEAVVRA IYNCKTPIIS AVGHETDFTL
SDFAADIRAA TPTQAAVIAT PDQYELLQQI QQYQFTLTRF IKKHLEQQRK HVEHLSSYYK
FKQPTLLYDQ QIQRRDDLEK RLKQQIQATF EQQRHRLMLL QQRYNLKALL SSVNQEQQNN
LQLTNQLVKL LNSKILSYKN DLKNKVENLN NLSPTNTMLR GYAIVNKKDE VITSTKDLTE
NDQLTLTMKD GLVDAKVTKV RCNND
