ID   EX7L_KLEP7              Reviewed;         463 AA.
AC   A6TCC4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=KPN78578_27840; ORFNames=KPN_02835;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR78245.1; -; Genomic_DNA.
DR   RefSeq; WP_015958798.1; NC_009648.1.
DR   AlphaFoldDB; A6TCC4; -.
DR   SMR; A6TCC4; -.
DR   STRING; 272620.KPN_02835; -.
DR   EnsemblBacteria; ABR78245; ABR78245; KPN_02835.
DR   KEGG; kpn:KPN_02835; -.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   Proteomes; UP000000265; 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; Reference proteome.
FT   CHAIN           1..463
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000048775"
SQ   SEQUENCE   463 AA;  52481 MW;  25F301D5AD4E65E0 CRC64;
     MLPSQSPAIF TVSRLNQTVR LLLEREMGQV WISGEISNFS QPSSGHWYFT LKDDNAQVRC
     AMFRNSNRRV TFRPQHGQQV LVRANITLYE PRGDYQIIVE SMQPAGEGLL QQKYEQLKAQ
     LTAEGLFEQK HKQALPSPAH CVGVITSKTG AALHDILHVL RRRDPGLPVI IYPTSVQGDD
     APGQIVRAIA LANARQECDV LIVGRGGGSL EDLWSFNDER VARAIFASQI PIVSAVGHET
     DVTIADFVAD LRAPTPSAAA EIVSRNQQEL LRQLQSGQQR LEMAMDYFLA SRQRRFTQLF
     HRLQQQHPQL RLARQQTALE RLRQRMRIAV ESQLKRAEQR QKRTVQRLNH YNPQPRIHRA
     QSRIQQLEYR LAEIMRGRLS ERRERFGNAV THLEAVSPLA TLARGYSVTS VSDGTVLKQT
     KQVKTGDLLT TRLKDGWVES EVKQIAPVKK TRARKPSPTK PAE