ID   THSA_BACDA              Reviewed;         494 AA.
AC   A0A5B8Z1N3;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 2.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=NAD(+) hydrolase ThsA {ECO:0000303|PubMed:34853457};
DE            Short=NADase ThsA {ECO:0000303|PubMed:34853457};
DE            EC=3.2.2.5 {ECO:0000250|UniProtKB:J8G6Z1};
DE   AltName: Full=Thoeris protein ThsA {ECO:0000303|PubMed:34853457};
GN   Name=thsA {ECO:0000305};
GN   ORFNames=FSZ17_06160 {ECO:0000312|EMBL:QED46885.1};
OS   Bacillus dafuensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1742359;
RN   [1] {ECO:0000312|EMBL:QED46885.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 43120 / FJAT-25496;
RA   Zheng X.;
RL   Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN ANTIVIRAL DEFENSE, AND EXPRESSION IN B.SUBTILIS.
RC   STRAIN=KCTC 43120 / FJAT-25496;
RX   PubMed=34853457; DOI=10.1038/s41586-021-04098-7;
RA   Ofir G., Herbst E., Baroz M., Cohen D., Millman A., Doron S., Tal N.,
RA   Malheiro D.B.A., Malitsky S., Amitai G., Sorek R.;
RT   "Antiviral activity of bacterial TIR domains via immune signalling
RT   molecules.";
RL   Nature 600:116-120(2021).
CC   -!- FUNCTION: Probable NAD(+) hydrolyzing component of antiviral defense
CC       system Thoeris, composed of ThsA, TIR1 (thsB1) and TIR2 (thsB2)
CC       (PubMed:34853457). Activated by a signal molecule generated by
CC       endogenous TIR1, TIR2 or ThsB from B.cereus. After activation it binds
CC       and hydrolyzes NAD(+), leading to cell death and inhibition of phage
CC       replication (Probable). Expression of Thoeris in B.subtilis (strain
CC       BEST7003) confers resistance to phages phi29, phi3T, SPBeta, SBSphi11,
CC       SBSphi13, SBSphiJ, SPO1 and SPR but not SBSphiC. The TIR paralogs
CC       confer overlapping resistance to different phages (PubMed:34853457).
CC       {ECO:0000269|PubMed:34853457, ECO:0000305|PubMed:34853457}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5;
CC         Evidence={ECO:0000250|UniProtKB:J8G6Z1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC         Evidence={ECO:0000250|UniProtKB:J8G6Z1};
CC   -!- ACTIVITY REGULATION: Probably activated by a signal molecule generated
CC       by endogenous TIR1 and/or TIR2. Can also be activated by the signal
CC       generated by ThsB of B.cereus. Activation may alter the oligomerization
CC       state of the protein. {ECO:0000305|PubMed:34853457}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=QED46885.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP042593; QED46885.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_057775117.1; NZ_CP042593.1.
DR   SMR; A0A5B8Z1N3; -.
DR   STRING; 1742359.GCA_001439625_04135; -.
DR   KEGG; bda:FSZ17_06160; -.
DR   Proteomes; UP000321555; Chromosome.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR039444; SIR2-like.
DR   InterPro; IPR041486; STALD.
DR   Pfam; PF13289; SIR2_2; 1.
DR   Pfam; PF18185; STALD; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..494
FT                   /note="NAD(+) hydrolase ThsA"
FT                   /id="PRO_0000456258"
SQ   SEQUENCE   494 AA;  56542 MW;  437DE986DC880B3C CRC64;
     MKIVLEEIAM ATDKEVLIKE FLKALHEDNA AIFAGAGLSA ASGFVNWKGL LKEAADELEL
     DIEKETDLIS LAQYFFNKNG RQRLSQLVID NFSAEAQLNE NHRILAQLPI DTYWTTNYDR
     LIEKSLTDVG KNPDVKIKQS DFALLKPKRD AIVYKMHGDI ERASETVLIK DEYEMFHENN
     QLFSIGLKGD LISKTFLFIG YSFEDPDLEY ILSRIRVLMG QDGRNHYCFF RKVNRNQYNH
     LPKEEGDEKF RYDSIKQELK CADLERYHIK PVLVDKYEDI TEILQTILQR YCRSKILISG
     SAVEYKQFVP DHNTAQMFIH TLSREMVKAG FKIASGFGLG VGSAVINGSL DYVYSTNKRK
     ISDYLILRPF PQYATNGLEL MDLWDQYRRD FISDVGCAVF IFGNKEVNGK VVDAGGVRKE
     FDIAVAQGIK VIPVGATGYM SKTLWEETIT NYDKYYSDFP ALKADFEFIG DASHNHHEII
     TRIIKIITAL RAGR