ID   EX7L_CAMFF              Reviewed;         387 AA.
AC   A0RMM6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=CFF8240_0255;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=82-40;
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-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; CP000487; ABK82191.1; -; Genomic_DNA.
DR   RefSeq; WP_011731750.1; NC_008599.1.
DR   AlphaFoldDB; A0RMM6; -.
DR   SMR; A0RMM6; -.
DR   STRING; 360106.CFF8240_0255; -.
DR   EnsemblBacteria; ABK82191; ABK82191; CFF8240_0255.
DR   GeneID; 61064099; -.
DR   KEGG; cff:CFF8240_0255; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_2_0_7; -.
DR   OMA; DFTIIDY; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000000760; 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..387
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000303778"
SQ   SEQUENCE   387 AA;  43715 MW;  DF186AA4BE7F3B0A CRC64;
     MTVSELNEQA KALLETHFSF VEVTGEISRL IRHSSGHWYF SLKDEKSVIS SAMYKFSNQQ
     VKFEVKDGMQ VTIYGKLTIY PPSGSYQLLA NKMLPVGIGE LELAFNQLKS KLENEGLFDI
     KFKKPLPKFP KKIAIVTSLT SAAYQDMLKV INSRYKLCEF IAFNTLVQGE MAAANIIQML
     QKADKMGFDA IVLARGGGSK EDLWCFNDEN LARVIFTLKT PIVSAVGHEI DYCISDFVSD
     HRSLTPTAAM VDLLPDANTI LQSLDIAFDK FESFIDGKFQ NSFNILNLIN QSLKNQAISQ
     KIEKANLTLE NKKANLENLI TSKINNLAHK IKEFELVFDR QEQFFKATKN MVQIEKNGKI
     MPLHELQIGD EISIYSQITK KNAIIKS