EX7L_STRPG
ID EX7L_STRPG Reviewed; 446 AA.
AC A2RDN0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=SpyM50620;
OS Streptococcus pyogenes serotype M5 (strain Manfredo).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=160491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Manfredo;
RX PubMed=17012393; DOI=10.1128/jb.01227-06;
RA Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT "Complete genome of acute rheumatic fever-associated serotype M5
RT Streptococcus pyogenes strain Manfredo.";
RL J. Bacteriol. 189:1473-1477(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; AM295007; CAM29955.1; -; Genomic_DNA.
DR RefSeq; WP_011017997.1; NC_009332.1.
DR AlphaFoldDB; A2RDN0; -.
DR KEGG; spf:SpyM50620; -.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
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..446
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303822"
SQ SEQUENCE 446 AA; 50553 MW; C1BA24606C2DF637 CRC64;
MADYLTVTHL TKYLKLKFDR DPYLERVYLT GQVSNFRKRP THQYFSLKDE SAVIQATMWA
GVYKKLGFDL EEGMKINVIG RVQLYEPSGS YSIVIEKAEP DGIGALALQF EQLKKKLTAE
GYFEQKHKQP LPQFVSKIGV ITSPSGAVIR DIITTVSRRF PGVEILLFPT KVQGDGAAQE
VVANIRRANQ REDLDLLIVG RGGGSIEDLW AFNEEIVVQA IFESQLPVIS SVGHETDTTL
ADFVADRRAA TPTAAAELAT PITKTDLMSW IVERQNRSYQ ACLRRIKQRQ EWVDKLSQSV
IFRQPERLYD AYLQKIDRLS MTLMNTMKDR LSSAKENKVQ LDHALANSQL QTKIERYQDR
VATAKRLLMA NMARQYDSQL ARFEKAQDAL LSLDVSRIIA RGYAMIEKNQ ALVASVSQIT
KGDQLTIKMR DGQLDVEVKD VKNENI
