EX7L_CAMJE
ID EX7L_CAMJE Reviewed; 387 AA.
AC Q9PIH4; Q0PBI4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=Cj0325;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL34476.1; -; Genomic_DNA.
DR PIR; A81452; A81452.
DR RefSeq; WP_002851089.1; NC_002163.1.
DR RefSeq; YP_002343763.1; NC_002163.1.
DR AlphaFoldDB; Q9PIH4; -.
DR SMR; Q9PIH4; -.
DR IntAct; Q9PIH4; 59.
DR STRING; 192222.Cj0325; -.
DR PaxDb; Q9PIH4; -.
DR PRIDE; Q9PIH4; -.
DR EnsemblBacteria; CAL34476; CAL34476; Cj0325.
DR GeneID; 904649; -.
DR KEGG; cje:Cj0325; -.
DR PATRIC; fig|192222.6.peg.317; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_7; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000000799; 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..387
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000197832"
SQ SEQUENCE 387 AA; 44088 MW; 10E3FD7D55FE9FBB CRC64;
MTPTELNLKA KALLETHFDD IVLSGEISKI TLHGSGHWYF DLKDERSSIA CAMFKGANLK
VGFKPAVGDF 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