EX7L_HELPG
ID EX7L_HELPG Reviewed; 420 AA.
AC B5ZA25;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=HPG27_238;
OS Helicobacter pylori (strain G27).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27;
RX PubMed=18952803; DOI=10.1128/jb.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI27005.1; -; Genomic_DNA.
DR RefSeq; WP_000558338.1; NC_011333.1.
DR AlphaFoldDB; B5ZA25; -.
DR EnsemblBacteria; ACI27005; ACI27005; HPG27_238.
DR KEGG; hpg:HPG27_238; -.
DR HOGENOM; CLU_023625_2_0_7; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001735; 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..420
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122066"
SQ SEQUENCE 420 AA; 47051 MW; 103221DED6E87A05 CRC64;
MHVLSVSEIN VQIKALLEAT FLQVRVQGEV SNLTIHKVSG HAYFSLKDSQ SVIRCVLFKG
NANRLKFALK EGQEMVVFGG ISVYVPRGDY QINCFEIEPK EIGSLTLALE QLKEKLRLKG
YFDEANKLPK PHFPKRVAVI TSQNSAAWAD MKKIASKRWP MCELVCINTL MQGEGCVQSV
VESIAYADSF HDTKNAFDAI VVARGGGSME DLYSFNDEKI ADALYLAKTF SMSAIGHESD
FLLSDLVADL RASTPSNAME ILLPNSDEWL QRLDGFNVKL CRSFKTLLHQ KKVHLEHLAA
SLKRLSFENK HHLNALKLEK LTIALENKTL EFLRLKKTLL EKISIQTLTS PFLQTKTERL
NRLENALKLA HANLKLPQFG ALVSKNNQAV ELEVLKAGDK IELSNEKARA SAEILSVDRV
