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Database: UniProt
Entry: A0A0R1XA58_9LACO
LinkDB: A0A0R1XA58_9LACO
Original site: A0A0R1XA58_9LACO 
ID   A0A0R1XA58_9LACO        Unreviewed;       456 AA.
AC   A0A0R1XA58;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=FC91_GL002792 {ECO:0000313|EMBL:KRM27010.1};
OS   Schleiferilactobacillus harbinensis DSM 16991.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Schleiferilactobacillus.
OX   NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM27010.1, ECO:0000313|Proteomes:UP000050949};
RN   [1] {ECO:0000313|EMBL:KRM27010.1, ECO:0000313|Proteomes:UP000050949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM27010.1,
RC   ECO:0000313|Proteomes:UP000050949};
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:KRM27010.1}.
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DR   EMBL; AZFW01000058; KRM27010.1; -; Genomic_DNA.
DR   RefSeq; WP_027828652.1; NZ_AZFW01000058.1.
DR   AlphaFoldDB; A0A0R1XA58; -.
DR   PATRIC; fig|1122147.4.peg.2878; -.
DR   eggNOG; COG1570; Bacteria.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000050949; 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   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:UP000050949}.
FT   DOMAIN          10..103
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          130..440
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   456 AA;  50174 MW;  9590CAABCC7A8F61 CRC64;
     MTETGRPEYL TVSALTEYIK RKFDADPYLG RIYVTGEVSN YRPRSGNQYF SLKDDKAKIN
     GMMFARDFAK VAFPVAEGMQ VAAIGRVSLY PPSGEYQLYV DELQPAGVGD LYVRFEALKK
     KLQTEGLFAR PKRPLPSFPR RIGVITSPSG AVIRDILTTA ARRDTLAQIV LFPAVVQGDA
     AASSLVQQLR QAYIHPNLDV LIIGRGGGSI EDLWPFNEES VARTMAESPL PLISSVGHET
     DTTIADMVAD VRAATPTAAA ELATPNVADL VLRIRQAANT LQATMQRRLT DTRGRVQQLV
     TAPVLRQPER LYALQTQHLD NLQQRLIGTT QNRLRQAEGT LAAANQRLWR QTPQNRVALA
     HQQAASDTQR LLAAQKALLQ QHRQTLRNGE HALDLLSPLR VLDRGYTYVT AADGTVIQQV
     SGVRPPQDVV LHFADGTATA QITATKKGQP NGNENK
//
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