ID   EX7L_LYSSC              Reviewed;         452 AA.
AC   B1HRX7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Bsph_3512;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA41000.1; -; Genomic_DNA.
DR   RefSeq; WP_012295059.1; NC_010382.1.
DR   AlphaFoldDB; B1HRX7; -.
DR   SMR; B1HRX7; -.
DR   EnsemblBacteria; ACA41000; ACA41000; Bsph_3512.
DR   KEGG; lsp:Bsph_3512; -.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000002164; 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..452
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000122072"
SQ   SEQUENCE   452 AA;  50991 MW;  2F5D56977EA2FDD6 CRC64;
     MSSASYLTVK ALTKYIKRKF DADPHLREVY VKGELSNVKI HQSGHIYFTL KDDGARIAAT
     MFKAAATKLA FEPKEGMQVF IRGDVNVYEG YGTYQLYVQE MQPDGIGSLF VAFNQLKEQL
     QKEGLFKLDW KQSIPKFPEK IGVLTSTTGA AIRDICTTLK RRYPLAEILI YPTLVQGAQA
     APNIVQNIQR ANQDATCQVL IVGRGGGSIE DLWAFNEEIV ARAIFESRIP IISAVGHETD
     TTIADYVSDL RAPTPTAAAE MAVPDQMELF QRVLSQKSQI HQMVRSQLMA ERQRLNKLQQ
     SYPLSMPERL YRPFTERLAQ LESGLQTAMQ VDLMKKSAQL QQLHSTVAQH SPKKALAFHQ
     RELEARMQQL TRAATYYVAK QQQQFEATIR TLEALNPLSI LTRGFTVAYK DQHMIKSSTE
     VQEQDYLTLA FHDGKVVAEV KDILPKNEGE SL