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Database: UniProt
Entry: A0A0R1ZBX2_9LACO
LinkDB: A0A0R1ZBX2_9LACO
Original site: A0A0R1ZBX2_9LACO 
ID   A0A0R1ZBX2_9LACO        Unreviewed;       447 AA.
AC   A0A0R1ZBX2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=FC64_GL001064 {ECO:0000313|EMBL:KRM51871.1};
OS   Ligilactobacillus araffinosus DSM 20653.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1423820 {ECO:0000313|EMBL:KRM51871.1, ECO:0000313|Proteomes:UP000051291};
RN   [1] {ECO:0000313|EMBL:KRM51871.1, ECO:0000313|Proteomes:UP000051291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20653 {ECO:0000313|EMBL:KRM51871.1,
RC   ECO:0000313|Proteomes:UP000051291};
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., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_00378,
CC         ECO:0000256|RuleBase:RU004355};
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}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|RuleBase:RU004355}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM51871.1}.
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DR   EMBL; AYYZ01000029; KRM51871.1; -; Genomic_DNA.
DR   RefSeq; WP_057906909.1; NZ_AYYZ01000029.1.
DR   AlphaFoldDB; A0A0R1ZBX2; -.
DR   STRING; 1423820.FC64_GL001064; -.
DR   PATRIC; fig|1423820.4.peg.1088; -.
DR   Proteomes; UP000051291; 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   NCBIfam; TIGR00237; xseA; 1.
DR   PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   Pfam; PF02601; Exonuc_VII_L; 1.
DR   Pfam; PF13742; tRNA_anti_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00378};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051291}.
FT   DOMAIN          7..101
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          128..437
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   COILED          271..299
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   447 AA;  51335 MW;  7F57A69A13E39E9F CRC64;
     MERKNYLTVT ALTKYIARKF TYDPYLERVY LIGEISNFRL RERHQYFSIK DENAKIEAVM
     FQSNFNRIKF VPEDGMKVLV TGRIEVYEQT GKYQINIETM QPDGVGALYQ AYEQLKAKLA
     QEGVFSRPKR SLVKFPKRIA VITSPSGAVI RDIITTTRRR YPIVQLVLFP AEVQGEYAKD
     SLVGRLKEVN ARGDFDTIII GRGGGSIEDL WPFNEEEVAR AIADSKIPVI SSVGHETDTT
     LSDLAADVRA ATPTAAAELA TPVLTDEILK LKDYQVRLAQ AMKRIIQLKQ QRLSKLEKSY
     IFRQPERLYD GFMQKIDLLE TRLLNNVQQK LQTEHQRLLV LNGKLQKCSP QQLIQDDRHR
     VDNLQDHLLE RIQNLMSMKE QQYLRANHAL ALLNPLNVMG RGFSYVTDPN DQVIKSVDSI
     TIHDQLNLHL KDGTAQVEVQ KIRKYQS
//
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