ID   PCTIR_RHOS2             Reviewed;         259 AA.
AC   A0A1V0HUU2;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Pycsar effector protein RsmPycTIR;
DE            Short=RsmPycTIR {ECO:0000303|PubMed:34644530};
DE            EC=3.2.2.5 {ECO:0000305|PubMed:34644530};
GN   Name=pycTIR {ECO:0000303|PubMed:34644530};
GN   ORFNames=B5V46_03435 {ECO:0000303|Ref.1};
OS   Rhodovulum sp. (strain MB263).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodovulum; unclassified Rhodovulum.
OX   NCBI_TaxID=308754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB263;
RA   Nagao N., Yonekawa C., Hiraishi A., Kikuchi Y., Hirose Y.;
RT   "Complete genome sequence of Rhodovulum sp. MB263.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROBABLE FUNCTION, AND CLASSIFICATION.
RC   STRAIN=MB263;
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:0000305|PubMed:34644530}.
CC   -!- FUNCTION: The effector gene of a two-gene Pycsar system. Expression of
CC       this and adjacent uridylate cyclase RsmPycC (AC A0A1V0HUX5) probably
CC       confers resistance to bacteriophage. The genes are probably only
CC       expressed in response to bacteriophage infection. Probably only
CC       responds to cUMP (produced by its cognate NTP cyclase), it may act by
CC       degrading NAD(+) and/or by impairing membrane integrity.
CC       {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: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DOMAIN: Has an N-terminal cyclic nucleotide-binding domain and a C-
CC       terminal transmembrane domain that may also be a Toll/interleukin-1
CC       receptor-like domain (TIR) that might have NAD(+) hydrolase activity.
CC       {ECO:0000305|PubMed:34644530}.
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DR   EMBL; CP020384; ARC87742.1; -; Genomic_DNA.
DR   EnsemblBacteria; ARC87742; ARC87742; B5V46_03435.
DR   KEGG; rhm:B5V46_03435; -.
DR   Proteomes; UP000191232; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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   Pfam; PF00027; cNMP_binding; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   3: Inferred from homology;
KW   Antiviral defense; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Nucleotide-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..259
FT                   /note="Pycsar effector protein RsmPycTIR"
FT                   /id="PRO_0000455239"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          126..229
FT                   /note="TIR-like"
FT                   /evidence="ECO:0000305|PubMed:34644530"
FT   BINDING         1..120
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
SQ   SEQUENCE   259 AA;  28329 MW;  8B82F81236F60061 CRC64;
     MVGGDEVIAN SFLEAGELVS FKRGEDIVSQ GDVEDDSVYF LLSGAADVFV NGKRRDDIQR
     TAPITVGEMS ALNPAQKRSA TVRAASRQLV ALKVEGETFR KVVGENREFL RRVHEDFSGR
     GRQAILATGI SRRTSGWNWT VISLTAGVLS AAAIWYTLRV DGNPVFVRVL LPLVVGLTIF
     LLTLLADPVY RFFRLGTLCV GAILVDEALQ WQVRGSFMGA EFQYQISSSG DPQQATALLA
     PIVLGALAAY LFWIDTTKR