ID   EX7L_STAAB              Reviewed;         445 AA.
AC   Q2YYB8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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}; OrderedLocusNames=SAB1396c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81085.1; -; Genomic_DNA.
DR   RefSeq; WP_001286923.1; NC_007622.1.
DR   AlphaFoldDB; Q2YYB8; -.
DR   SMR; Q2YYB8; -.
DR   KEGG; sab:SAB1396c; -.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OMA; WPAVRFE; -.
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.
FT   CHAIN           1..445
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000273695"
SQ   SEQUENCE   445 AA;  50908 MW;  8F1ACB33D061A4F1 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 HIEHLSSYYK
     FKQPTLLYDQ QIQRRDDLEK RLKQQIQATF EQQRHRLMLL QQRYNLKALL SSVNQEQQNN
     LQLTNQLVKL LNSKILSYKN DLKNKVENLN NLSPTNTMLR GYAIVNKKDE VITSTKDLTE
     NDQLTLTMKD GLVDAKVTKV RCNND