ID   EX7L_LEPBJ              Reviewed;         422 AA.
AC   Q04TB1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-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=LBJ_1274;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000350; ABJ75859.1; -; Genomic_DNA.
DR   RefSeq; WP_011670154.1; NC_008510.1.
DR   AlphaFoldDB; Q04TB1; -.
DR   SMR; Q04TB1; -.
DR   EnsemblBacteria; ABJ75859; ABJ75859; LBJ_1274.
DR   KEGG; lbj:LBJ_1274; -.
DR   HOGENOM; CLU_023625_3_1_12; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000000656; Chromosome 1.
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..422
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000303795"
SQ   SEQUENCE   422 AA;  47095 MW;  07627BCB9A216F02 CRC64;
     MEDSKPLTVS EVTRILKNLI TGSKDLKNIW VRGEISNYSK ASSGHIYFSL KDSSSLMRCT
     FFNYSNKNYS GKPLSDGKEV QVYGTVTLYE AGGSYNLNVA RVEELGQGDI LLQIEKLKQK
     LAAEGIFDPE RKRRIPSFPK TLGIATSPSG AAIEDIIKIA RSRFPGINIL ISPCFVQGDE
     APDSIVAAIE ELNHPSWGVD VIIAGRGGGS FEDLMAFNDE KVVRAYANSR IPIISAVGHQ
     TDVLLSDFAA DYSTPTPTAA AEYAVPKEED VLQFLTQLEG RLKTSLLAKI SSSKDRLRLL
     SGKFIFKEPM QLLNQRNQRV DEIGVRLQKA VFNKVGLARV RLERYEDLTS RMRNIFFHKK
     QKAEFWTTKV EDLSPPATMK RGYSILRNQK GKIIRSPEET KPEEELQVLL SGGTMQVIRK
     GK