ID   EX7L_LACLM              Reviewed;         417 AA.
AC   A2RLU4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=llmg_1692;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(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; AM406671; CAL98266.1; -; Genomic_DNA.
DR   RefSeq; WP_011835498.1; NZ_WJVF01000033.1.
DR   AlphaFoldDB; A2RLU4; -.
DR   SMR; A2RLU4; -.
DR   STRING; 416870.llmg_1692; -.
DR   EnsemblBacteria; CAL98266; CAL98266; llmg_1692.
DR   KEGG; llm:llmg_1692; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OMA; WPAVRFE; -.
DR   PhylomeDB; A2RLU4; -.
DR   BioCyc; LLAC416870:LLMG_RS08515-MON; -.
DR   Proteomes; UP000000364; 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..417
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000303794"
SQ   SEQUENCE   417 AA;  47149 MW;  9B3B5850A8CCB639 CRC64;
     MTEYLSVSTL TKYLKAKFER DPYLERVYLT GEISNFRRRP NHQYFALKDE GAVIQATMWA
     GQFRKLDFEL EEGMKVLAIG RISIYPPSGS YSINIESLVP DGVGALALKF EQLKKKLAAE
     GLFDQRWKQN LPQFSKKIAV VTSPSGAVIR DIITTVQRRF PMSQIVLYPT KVQGAGAAEE
     ISGNIRRANE RGDFDVMIIG RGGGSIEDLW GFNEEIVVRA IFESRIPIIS SVGHETDVTL
     ADFVADSRAA TPTAAAELAT PNTKIDLINW ANEQESRLFN RLTHLIKIRR ERLEKLSQSV
     VFRQPERLYD GHVQKLDRLC ERLTVLTENK VANMKHRYEL SANRLIPTYS KIVESKKNKT
     EQLYQSLLLL DISKIKARGF SLITDENGKI IKSVSDVKKG QALDVELTDG QVKVEVK