ID   EX7L_BART1              Reviewed;         476 AA.
AC   A9IXA1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=BT_1859;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105476 / IBS 506;
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems as
RT   host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK02136.1; -; Genomic_DNA.
DR   RefSeq; WP_012232214.1; NC_010161.1.
DR   AlphaFoldDB; A9IXA1; -.
DR   SMR; A9IXA1; -.
DR   STRING; 382640.BT_1859; -.
DR   EnsemblBacteria; CAK02136; CAK02136; BT_1859.
DR   KEGG; btr:BT_1859; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_5; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000001592; 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..476
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000079974"
SQ   SEQUENCE   476 AA;  52904 MW;  335560B861FCB4F7 CRC64;
     MVNLLSEKTS GTNVAEFTVS EIAGALKRVV EEKFGYVRVR GEISGYRGAH ASGHAYFALK
     DDKARLEAVI WRGVMEKLKF PPEEGMEVVA VGKLTTYPGS SKYQIVIEAL EPTGVGALMT
     LLENRKKKFA EEGLFDEAKK KPLPYMPRII GVVTSPTGAV IRDIIHRISD RFPLHVLVWP
     VRVQGETSGS EVAAAVEGFN ALASEGHIPK PDLIIVARGG GSLEDLWGFN DEAVVRAVYA
     SDLPIISAVG HETDWTLIDY VADWRAPTPT GAAEKAVPVK LDLEVCVASL GARLRKGLAR
     SFDFHQQKLC AARRGLPSAD QLFSLPRRGF DEISSRLQRA LCVSYDKKRF SFHALHLRLS
     PRLLKSEKAQ RHTKEYTARL YRAFMRSVEK KRSALELACR LLKSTSYQNI LERGFVLVLG
     QNHKPIKRLA QFPESGQINL RFFDGDIHVA TQEPFSAARS KHKKIKSPSD DQGTLF