EX7L_LIGS1
ID EX7L_LIGS1 Reviewed; 446 AA.
AC Q1WUJ2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=LSL_0534;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99343.1; -; Genomic_DNA.
DR RefSeq; WP_011475809.1; NC_007929.1.
DR RefSeq; YP_535426.1; NC_007929.1.
DR AlphaFoldDB; Q1WUJ2; -.
DR STRING; 362948.LSL_0534; -.
DR PRIDE; Q1WUJ2; -.
DR EnsemblBacteria; ABD99343; ABD99343; LSL_0534.
DR KEGG; lsl:LSL_0534; -.
DR PATRIC; fig|362948.14.peg.612; -.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000006559; 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_0000273666"
SQ SEQUENCE 446 AA; 50797 MW; E44AE6B2C162C6E4 CRC64;
MSKEYLTVSA LTKYLHTKFT RDPYLRRVYL TGEISNFRRR ATHQYFSLKD DNAVISVMMF
QSAFSKIKFE PEKGMKVLVS GRVDLYEKSG RYQIIIDTMQ PDGVGALYQA YEQLVKKLRI
EGLFNEELKK PLVKYPKRIA VITSPSGAVI RDIITTTHRR YPIAQLVLFP AVVQGDDAAD
SLVGRLKQVN EEGNFDTIII GRGGGSIEDL WPFNEEKVAR AISDSKIPVI SSVGHETDTT
IADLVADVRA ATPTAAAELA TPVLSEEIVK IKQYRLRIIQ VLKNKISNYQ QILDKVCSSY
ILQQPDRLYT GYAQNLDSLI NRKNQAFKNL VYQNEKQLQL LESNLQHNNP SIRIKDEKNN
LQQLLEKMHL GMLGVFNDKS YKLEKLMSSL DMLSPLKVMN RGYSYILKDG KTVKNVKSLQ
PNDDVTLYFE NGSAEARITK IREEKE
