EX7L_BACC1
ID EX7L_BACC1 Reviewed; 452 AA.
AC Q731B3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=BCE_4253;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS43154.1; -; Genomic_DNA.
DR RefSeq; WP_000415266.1; NC_003909.8.
DR AlphaFoldDB; Q731B3; -.
DR SMR; Q731B3; -.
DR EnsemblBacteria; AAS43154; AAS43154; BCE_4253.
DR GeneID; 59155246; -.
DR GeneID; 64199530; -.
DR KEGG; bca:BCE_4253; -.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000002527; 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_0000273640"
SQ SEQUENCE 452 AA; 51368 MW; 567F37FA7A57846E CRC64;
MEKQYLTVTA LTRYIKTKIE YDPHLQSVWL KGEISNFKNH SRGHMYFTLK DENARIAAVM
FAGHNRNIKF RPENGMKVLV KGKISVYEAS GSYQIYIQDM QPDGVGNLHL AYEQLKVRLE
EEGLFSQVYK KTIPPYAKTI GVITSPTGAA IRDIITTIKR RYPIGNVIVF PVLVQGESAA
PSIVQAIRTA NEMEGIDVLI VGRGGGSIEE LWAFNEEMVA RAIFKSEIPI ISAVGHETDF
TIADFVADLR APTPTAAAEL AAPNIIELQE KVLQRTLRLQ RAMRELVHKK EEKLQVLQKS
YAFRYPRQVY EQKEEQLDRA LEQLVLAKER YIDKKVNQLK QLSFYLEKHH PSQKIMQTKV
AVETLQKQLQ REMQTLLQTK EFAFVRAAQK LEALSPLKVM MRGYGLVYDE EKQVLKSVKD
VSLGDAVSVQ LQDGILDCSV SGIEERELNN GK
