ID   EX7L_STAHJ              Reviewed;         445 AA.
AC   Q4L6M4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 115.
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=SH1392;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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_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; AP006716; BAE04701.1; -; Genomic_DNA.
DR   RefSeq; WP_011275688.1; NC_007168.1.
DR   AlphaFoldDB; Q4L6M4; -.
DR   SMR; Q4L6M4; -.
DR   STRING; 279808.SH1392; -.
DR   PRIDE; Q4L6M4; -.
DR   EnsemblBacteria; BAE04701; BAE04701; SH1392.
DR   KEGG; sha:SH1392; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_2_0_9; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000000543; 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.
FT   CHAIN           1..445
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000197885"
SQ   SEQUENCE   445 AA;  51310 MW;  08F5B65151660151 CRC64;
     MSEYLSVTTL TKYIKYKFDQ DPHLQSILLK GELSNFKKHS SGHLYFNVKD KDSVISAMMF
     KGNANQLTFE PKEGDEVLLE ARVSVYERRG NYQIYVNKME LDGIGNLYQK LEQLKQKLKK
     EGFFNNEHKK PIPRFPKKIA ILTASTGAAI RDIQSTINSR YPLAEKIQIS TLVQGTQAKE
     DIIKNIKYAD SLGVDTIIVG RGGGSIEDLW NFNEEDVVKA IFECQTPIIS AVGHETDFTL
     SDFVADVRAA TPTQAAVMAT PDQYELMQQI KQYQFSLSRY IKQYLEKQYK QLDHLASYYK
     FKQPSLLYDQ QIQRKDDLER QLTQLLLSKI ENKKYQLKVL HQNFNVKTLN QTILQNKRQL
     VNVKNRLSNL TMKNIHNNKL EFKNKVELLN NLSPTNTMLR GYSIINKDDK VITSTQDLSK
     DDEITLAMKD GNVDAIVKKV RCEHE