ID   PCTIR_XANPE             Reviewed;         303 AA.
AC   P0DV29;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Pycsar effector protein XpPycTIR;
DE            Short=XpPycTIR {ECO:0000303|PubMed:34644530};
DE            EC=3.2.2.5 {ECO:0000305|PubMed:34644530};
DE   AltName: Full=NAD(+) hydrolase;
GN   Name=pycTIR {ECO:0000303|PubMed:34644530};
GN   ORFNames=GEV1001_09740 {ECO:0000303|PubMed:26089818};
OS   Xanthomonas perforans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=442694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GEV1001;
RX   PubMed=26089818; DOI=10.3389/fmicb.2015.00535;
RA   Schwartz A.R., Potnis N., Timilsina S., Wilson M., Patane J.,
RA   Martins J. Jr., Minsavage G.V., Dahlbeck D., Akhunova A., Almeida N.,
RA   Vallad G.E., Barak J.D., White F.F., Miller S.A., Ritchie D., Goss E.,
RA   Bart R.S., Setubal J.C., Jones J.B., Staskawicz B.J.;
RT   "Phylogenomics of Xanthomonas field strains infecting pepper and tomato
RT   reveals diversity in effector repertoires and identifies determinants of
RT   host specificity.";
RL   Front. Microbiol. 6:535-535(2015).
RN   [2]
RP   FUNCTION AS AN NAD HYDROLASE, ANTIVIRAL DEFENSE, INDUCTION, AND
RP   CLASSIFICATION.
RC   STRAIN=GEV1001;
RX   PubMed=34644530; DOI=10.1016/j.cell.2021.09.031;
RA   Tal N., Morehouse B.R., Millman A., Stokar-Avihail A., Avraham C.,
RA   Fedorenko T., Yirmiya E., Herbst E., Brandis A., Mehlman T.,
RA   Oppenheimer-Shaanan Y., Keszei A.F.A., Shao S., Amitai G., Kranzusch P.J.,
RA   Sorek R.;
RT   "Cyclic CMP and cyclic UMP mediate bacterial immunity against phages.";
RL   Cell 0:0-0(2021).
CC   -!- FUNCTION: Pycsar (pyrimidine cyclase system for antiphage resistance)
CC       provides immunity against bacteriophage. The pyrimidine cyclase (PycC)
CC       synthesizes cyclic nucleotides in response to infection; these serve as
CC       specific second messenger signals. The signals activate the adjacent
CC       effector, leading to bacterial cell death and abortive phage infection.
CC       A clade B Pycsar system. {ECO:0000269|PubMed:34644530}.
CC   -!- FUNCTION: The effector gene of a two-gene Pycsar system. Expression of
CC       this and adjacent uridylate cyclase XpPycC (AC P0DV28) confers
CC       resistance to bacteriophage T7. When cells expressing the Pycsar system
CC       are infected by phage T7 at low multiplicity of infection (0.2 MOI) the
CC       culture survivey, at 2.0 MOI bacteria enter growth arrest. The same
CC       cells enter growth arrest after exposure to 2.5 mM cUMP but not cCMP;
CC       the effector protein responds only to the cUMP usually produced by its
CC       cognate NTP cyclase. NAD(+) levels in infected cells are depleted
CC       between 5 and 10 minutes after infection with T7 at MOI of 2
CC       (PubMed:34644530). Probably only responds to cUMP (Probable).
CC       {ECO:0000269|PubMed:34644530, ECO:0000305|PubMed:34644530}.
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:0000305|PubMed:34644530};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: In E.coli strain MG1655 transformed with both genes NAD(+)
CC       levels fall dramatically by 10 minutes after infection with phage T7
CC       (at protein level). {ECO:0000269|PubMed:34644530}.
CC   -!- DOMAIN: Has an N-terminal cyclic nucleotide-binding domain and a C-
CC       terminal Toll/interleukin-1 receptor-like domain (TIR) that probably
CC       has the NAD(+) hydrolase activity. {ECO:0000305}.
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DR   EMBL; JZVV01000016; KLD05782.1; -; Genomic_DNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR019302; TIR-like_dom.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF10137; TIR-like; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Cytoplasm; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..303
FT                   /note="Pycsar effector protein XpPycTIR"
FT                   /id="PRO_0000455241"
FT   REGION          154..273
FT                   /note="TIR-like"
FT                   /evidence="ECO:0000305|PubMed:34644530"
FT   BINDING         14..138
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
SQ   SEQUENCE   303 AA;  33779 MW;  2EB382DF96229DB1 CRC64;
     MIERFQGDEG RRRLVATLTE HRLVANRQEL AERLVAVGEL MEAPAGTTFI NQGDQTSEVF
     FIIAGKVEVR VNGKVVANRF PGDSVGEMAA IEPSQPRAAS VIPVEDTVLI KVSEAEFSAA
     AEQFPDVWRR IAATLARRLA ERNHLVTAQR ERVRVFIMSS VEALPIVDLL IKQFAHDPFL
     AVAWKNGVFR ASQYTLDELE AELDDSDFAV AVAHGDDVLI TRDDEWPTIR DNVILEFGLF
     MGRLGRRRAF LMEPRDVDLK LPSDLAGLTT IPYRYVKGKD AEHYIAPACA RLRELILAAG
     AKD