EX7L_STACT
ID EX7L_STACT Reviewed; 446 AA.
AC B9DNP9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Sca_1147;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(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; AM295250; CAL28055.1; -; Genomic_DNA.
DR RefSeq; WP_015900396.1; NC_012121.1.
DR AlphaFoldDB; B9DNP9; -.
DR SMR; B9DNP9; -.
DR STRING; 396513.SCA_1147; -.
DR GeneID; 60545163; -.
DR KEGG; sca:SCA_1147; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR BioCyc; SCAR396513:SCA_RS05745-MON; -.
DR Proteomes; UP000000444; 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..446
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200680"
SQ SEQUENCE 446 AA; 50866 MW; 52F2B90424B5AF97 CRC64;
MSDYLSVTAL TKYIKYKFDQ DPHLQSVLLK GELSNFKKHS SGHLYFNLKD NNSVVNAMMF
KAQANKLDFN PKEGDEVLIE ARVSVYERQG NYQIYVNKMH LDGIGNLYQK LEALKKELKK
QGLFDTKHKK EIPRFPKKIA VLTASTGAAI RDIYSTINSR YPLVEQIQIS TLVQGKQAKD
DIVNKIKYAD TLDADVMIVG RGGGSIEDLW NFNEEEVVRA IFEAKTPVIS AVGHETDFTL
SDFVADVRAA TPTQAAVIAT PDQVELSQYI KQTELNLSRH IIQIINNKKK HLEHVASYYK
FKQPSLLYDQ QIQKKDDFER QLNLSITTKL NNALQKVELL TNRINLKDLK QQTLQGIQSR
LQLHDSLNKS IINIIDNSKK RLSQRIENLN SLSPSNTMLR GYTIVNKNEQ VITSTQSLEK
NDEINLQMKD GTVDAIVKKV RCNHNE
