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   27-MAR-2024, entry version 87.
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};
GN   OrderedLocusNames=Sca_1147;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Bacillota; 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   GeneID; 60545163; -.
DR   KEGG; sca:SCA_1147; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OrthoDB; 9802795at2; -.
DR   BioCyc; SCAR396513:SCA_RS05745-MONOMER; -.
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   NCBIfam; TIGR00237; xseA; 1.
DR   PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   Pfam; PF02601; Exonuc_VII_L; 1.
DR   Pfam; PF13742; tRNA_anti_2; 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
//