EX7L_LACCB
ID EX7L_LACCB Reviewed; 449 AA.
AC B3WEY3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=LCABL_18540;
OS Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=543734;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL23;
RA Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA Deutscher J.;
RT "Lactobacillus casei BL23 complete genome sequence.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; FM177140; CAQ66934.1; -; Genomic_DNA.
DR RefSeq; WP_012491654.1; NC_010999.1.
DR AlphaFoldDB; B3WEY3; -.
DR KEGG; lcb:LCABL_18540; -.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
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..449
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122069"
SQ SEQUENCE 449 AA; 50304 MW; 4C5C4A6D71652D27 CRC64;
MVDASQYLSV TALTQYLKRK FDADPYLAKV YLTGEISNYR KRVGNQYFSL KDDHAKIGAL
MFRNAFSKVQ FDLEEGMKVL VVGRVSLYEP SGEYRLIVEH LEPDGVGALY QAFEQLKKKL
AAEGLFDRNQ RPLPLFPKRV AVVTSPSGAV IQDIMTTVAR RYPILQLTLF PAVVQGDQAA
DSLVKRLNQI KTIGGFDAVI IGRGGGSIED LWPFNEEKVA RALVDMPMPV VSSVGHETDT
TITDFIADRR AATPTAAAEI VTPVTLIDAL NRISEDRVRL VNAMHNRLKN AAIRVQRSAQ
SVVLTQPDRL YDQYVQRVDQ FQQRLQQSMH NRLREADHRL AMAASQLDGR QLFIRLVNLQ
RQVTGDRHRL DQAMRGLVKT KRQAFASAVS GLDHLSPLKI LGRGFAYVTD EQGQMLKSLS
DYELDQDIHI HVADGQVGAH VTTKEKTHG