ID   EX7L_MYCBT              Reviewed;         415 AA.
AC   C1AMA2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, 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=JTY_1141;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT   Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL   Vaccine 27:1710-1716(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; AP010918; BAH25431.1; -; Genomic_DNA.
DR   RefSeq; WP_003405846.1; NZ_CP014566.1.
DR   AlphaFoldDB; C1AMA2; -.
DR   SMR; C1AMA2; -.
DR   GeneID; 45425082; -.
DR   KEGG; mbt:JTY_1141; -.
DR   HOGENOM; CLU_023625_2_1_11; -.
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; 2.
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..415
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000200673"
SQ   SEQUENCE   415 AA;  44628 MW;  2182DA0BD1E278B4 CRC64;
     MTQNSAENPF PVRAVAIRVA GWIDKLGAVW VEGQLAQITM RPDAKTVFMV LRDPAADMSL
     TVTCSRDLVL SAPVKLAEGV QVVVCGKPSF YTGRGTFSLR LSEIRAVGIG ELLARIDRLR
     RLLDAEGLFD PRLKRPIPYL PNMIGLITGR ASAAERDVTT VASARWPAAR FAVRNVAVQG
     PNAVGQIVEA LRELDRDPDV DVIVLARGGG SVEDLLPFSD ETLCRAIAAC RTPVVSAVGH
     EPDNPLCDLV VDLRAATPTD AAKKVVPDTA AEQRLIDDLR RRSAQALRNW VSREQRAVAQ
     LRSRPVLADP MTMVSVRAEE VHRARSTLRR NLTLMVAAET ERIGHLAARL ATLGPAATLA
     RGYAIVQTVA QTGPEGGSEP QVLRSVHDAP EGTKLRVRVA DGALAAVSEG QTNGL