ID   EX7L_STRSV              Reviewed;         446 AA.
AC   A3CLQ7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SSA_0674;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(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; CP000387; ABN44112.1; -; Genomic_DNA.
DR   RefSeq; WP_011836653.1; NC_009009.1.
DR   RefSeq; YP_001034662.1; NC_009009.1.
DR   AlphaFoldDB; A3CLQ7; -.
DR   STRING; 388919.SSA_0674; -.
DR   PRIDE; A3CLQ7; -.
DR   EnsemblBacteria; ABN44112; ABN44112; SSA_0674.
DR   KEGG; ssa:SSA_0674; -.
DR   PATRIC; fig|388919.9.peg.649; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000002148; 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..446
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000303823"
SQ   SEQUENCE   446 AA;  50952 MW;  C8C24542D91F5A6D CRC64;
     MPEYLSVSTL TKYLKMKFER DPYLERVYLT GQVSNFRRRP NHQYFSLKDE KAVIQVTIWS
     GVYQKLGFEL EEGMKINVIG RVQLYEPSGS YSIIIEKAEP DGIGALAIQF EQLKKKLGEE
     GLFQDKFKQA LPQFPKKIGV VTSPSGAVIR DIITTVSRRF PGVEIVLYPT KVQGDGAAAQ
     VADHIRLANE RSVLDVLIIG RGGGSIEDLW AFNEEKTVRA IFESRIPVIS SVGHETDTTL
     ADFVADHRAA TPTAAAELAT PVTKLDLLGH LQQQENRMSR AISNRLSYYR ERLNKLTQSV
     IFRQPERLYD GHLQKLDQLN LRLKQKIREY YSEEQQRVKI LQHRLEALNP LSRVQHLQEQ
     TAQLERLLRS NMAVIYDNKV AQVRRLSEAL LMLDTSRIVA RGYAIVQKNQ KVIESSAGIE
     EKDELTLLMR DGQLEVEVKH VQRKEI