THSB2_BACDA
ID THSB2_BACDA Reviewed; 379 AA.
AC A0A5B8Z260;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Thoeris protein TIR2 {ECO:0000303|PubMed:34853457};
GN Name=thsB2 {ECO:0000305};
GN ORFNames=FSZ17_06170 {ECO:0000312|EMBL:QED46887.1};
OS Bacillus dafuensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1742359;
RN [1] {ECO:0000312|EMBL:QED46887.1}
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, FUNCTION, ACTIVITY REGULATION, AND
RP 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: One of 2 TIR-like protein components of antiviral defense
CC system Thoeris, composed of ThsA, TIR1 (thsB1) and TIR2 (thsB2). Phage
CC infection activates this protein; by 70 minutes post-infection with
CC phage SPO1, TIR2 generates a signal molecule that in turn activates the
CC NAD(+) hydrolase activity of ThsA (tested with B.cereus). The signal is
CC similar to cyclic ADP-D-ribose, but how it differs is unknown.
CC Expression of Thoeris in B.subtilis (strain BEST7003) confers
CC resistance to phages phi29, phi3T, SPBeta, SBSphi11, SBSphi13, SBSphiJ,
CC SPO1 and SPR but not SBSphiC. The TIR paralogs confer resistance to
CC different phages; this subunit confers resistance to phi3T, SPBeta,
CC SBSphi13, SBSphiJ, SPO1 and SPR but not phi29, SBSphi11 or SBSphiC.
CC There is overlap in the phage range for this system, both TIR1 and TIR2
CC are activated by SBSphi13, SBSphiJ, SPO1 and SPR.
CC {ECO:0000269|PubMed:34853457}.
CC -!- ACTIVITY REGULATION: Activated upon phage infection.
CC {ECO:0000305|PubMed:34853457}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; CP042593; QED46887.1; -; Genomic_DNA.
DR RefSeq; WP_057775113.1; NZ_CP042593.1.
DR SMR; A0A5B8Z260; -.
DR KEGG; bda:FSZ17_06170; -.
DR Proteomes; UP000321555; Chromosome.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IEA:UniProt.
DR GO; GO:0019677; P:NAD catabolic process; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF13676; TIR_2; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Reference proteome.
FT CHAIN 1..379
FT /note="Thoeris protein TIR2"
FT /id="PRO_0000456262"
FT DOMAIN 254..379
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ SEQUENCE 379 AA; 45088 MW; 867AA4AAF2A4EEA9 CRC64;
MPGVAKRKYV GETMRINKNL SQVLRRLSDV LPYNYNAETL LELFQQLYPH EWRELNQRFD
QYKEKDEFLL KKGKKIRYKP NPPKEHFFKL PIVKNILSKG RIAKHNANFD ELAYQERFAK
FKAKRENAIR SRNEKIAKAN ELIQNVEPLF IDTFIAAYHK RGISFDEKME IFKELQKYKS
KKTAEFFYKL SESERNNQIR NMAFKHLQVT GNYVKLRKNF NGKKKEYMTE SSEFFMTPLD
LLKRIESNNV QNKKVYDVFI SHSYKDSSVI KKIIKAFNKL SISIYCDWTS DSDFLKRELV
SEYTKVVLKK RIEQSKNIVF VKTDNSLESH WVRFELDYSR ELGKTLFCIN LSDEAEGECN
VLQFDVKNET ISWTTGLVK