ID   EX7L_RICBR              Reviewed;         442 AA.
AC   Q1RK25;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=RBE_0208;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(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; CP000087; ABE04289.1; -; Genomic_DNA.
DR   RefSeq; WP_011476902.1; NC_007940.1.
DR   AlphaFoldDB; Q1RK25; -.
DR   SMR; Q1RK25; -.
DR   STRING; 336407.RBE_0208; -.
DR   EnsemblBacteria; ABE04289; ABE04289; RBE_0208.
DR   KEGG; rbe:RBE_0208; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_2_0_5; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000001951; 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..442
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000273121"
SQ   SEQUENCE   442 AA;  49474 MW;  0B31507C46A20525 CRC64;
     MLDNFTSSQT TKEFSVSEIS NKIKELLENN FGYIKVKGEI SGLKIASSGH AYFNLKENTA
     ILACTCWRPI LAKIKFPLND GMEVVISGKL SSYAGNSRYQ LSVENLQPAG LGAMVQILNE
     RKARLEKEGL FNKIRKPIPF LPNKIGVITS ITGAVIQDII HRIRERFPTH VIIWPVSVQG
     ENSGNEIAEA IDGFNKLEEA NKPDVIIVAR GGGSIEDLWS FNDEVLVRAT YNSKIPIISA
     VGHEVDYTLI DLAADKRAPT PTAAAEFAVP VRSILNSTLQ SYEKVLVTNT KQLVKNHEQA
     ITNYDKINRY LAHYINHKQQ LLDETGFNLL DSLPCLISLK ETKLKSFSKE RIHPHKIITY
     KTLELTHKAA YIIKSANNTL KNFEYKLELN SLLLLSLDYH NVLKRGFAIV KGESGNFVSS
     KTTTEKVLNI QFFDGNIKAV RD