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Database: UniProt
Entry: A0A0R2A5V6_9LACO
LinkDB: A0A0R2A5V6_9LACO
Original site: A0A0R2A5V6_9LACO 
ID   A0A0R2A5V6_9LACO        Unreviewed;       451 AA.
AC   A0A0R2A5V6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378};
DE   AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
GN   Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378};
GN   ORFNames=FD44_GL001251 {ECO:0000313|EMBL:KRM59627.1};
OS   Lactobacillus malefermentans DSM 5705 = KCTC 3548.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1122149 {ECO:0000313|EMBL:KRM59627.1, ECO:0000313|Proteomes:UP000051712};
RN   [1] {ECO:0000313|EMBL:KRM59627.1, ECO:0000313|Proteomes:UP000051712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5705 {ECO:0000313|EMBL:KRM59627.1,
RC   ECO:0000313|Proteomes:UP000051712};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
RA   Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
RA   Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
RA   Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through
RT   comparative genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large
CC       acid-insoluble oligonucleotides, which are then degraded further
CC       into small acid-soluble oligonucleotides. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|SAAS:SAAS00723532}.
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to
CC       3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
CC       {ECO:0000256|HAMAP-Rule:MF_00378, ECO:0000256|RuleBase:RU004355,
CC       ECO:0000256|SAAS:SAAS00723505}.
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00378}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
CC       ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723552}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|RuleBase:RU004355,
CC       ECO:0000256|SAAS:SAAS00723548}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRM59627.1}.
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DR   EMBL; AZGJ01000004; KRM59627.1; -; Genomic_DNA.
DR   EnsemblBacteria; KRM59627; KRM59627; FD44_GL001251.
DR   PATRIC; fig|1122149.3.peg.1295; -.
DR   Proteomes; UP000051712; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000051712};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|SAAS:SAAS00723549};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723511};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723558};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723518}.
FT   DOMAIN        9    104       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      131    439       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
SQ   SEQUENCE   451 AA;  51312 MW;  FFF9C0B9493BCA15 CRC64;
     MIKVADDYLT VSALTQYLKR KFDVDPYLNR VYLTGEISNF RLRRNAHQYF SIKDDHAKIS
     AIMFKSAFEK IKFEPEEGMK VLVTGRISLY EQTGNYQIYV DHMEPDGVGQ FYQAYEQLKK
     KLDAEGLFTA PKKPLVQFPK RIAVVTSPSG AVIRDIITTT RRRFPISQIV LFPAIVQGND
     AADNLVQQIN RINDLGTFDT MIVGRGGGSI EDLWPFNEER VARAIFNSKI PVISSVGHET
     DTTIADLVAD VRAATPTAAA ELAVPVLSDL VANILQMRTR LVSVMQSRLT SEQQRLTKLS
     SSYIFQQPER LYQGYSQNVD LLRDRLKRKM QTQLNGWEHQ ISLIHQRLYS ASPTDSVRRA
     NQTLRDLNFR QNRAIKLELE NKKRKFTDSV SRLDALSPLR TMSRGYGYLT ENGKVLKTTN
     DLKLNQKVTI QLIDGTAKAK IEQIETTKGE K
//
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