EX7L_CAMJJ
ID EX7L_CAMJJ Reviewed; 387 AA.
AC A1VY44;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=CJJ81176_0347;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-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; CP000538; EAQ73041.1; -; Genomic_DNA.
DR RefSeq; WP_002859429.1; NC_008787.1.
DR AlphaFoldDB; A1VY44; -.
DR SMR; A1VY44; -.
DR STRING; 354242.CJJ81176_0347; -.
DR EnsemblBacteria; EAQ73041; EAQ73041; CJJ81176_0347.
DR KEGG; cjj:CJJ81176_0347; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_7; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000000646; 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_0000303779"
SQ SEQUENCE 387 AA; 44087 MW; FD8075D477F8D959 CRC64;
MTPTELNLKA KALLETHFDD IVLSGEISKI TLHGSGHWYF DLKDERSSIA CAMFKGANLK
VGFKPAVGNF LELCGSVSLY PESGRYQFIA TSMKKAGFGD LEAQFLALKE RLQKEGLFDP
RFKKSLPKFP KKVGIITSKT SAALQDMLKL IHQKEYFLAK IYIFDALTQG NNAPFSLIQA
LKKADDMDLD VLIIARGGGS REDLFCFNDE NLAREIFKAK TPIISAIGHE IDYVISDFVA
DFRAPTPSAA IDTLFYSKLD IEQSLDLMEE KLMQLWNYKI QNYENLLLNL SKFFKFNSLP
KIIDEKIKQS HNIEKQLNHL LANQMRYNEL KLDKLQNAYL QHENFFNKSK KFICIRKNGK
IANLEDLKSD DIVILSSQTS QKEAKIL
