ID   PCTM_STAAU              Reviewed;         158 AA.
AC   P0DV39;
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 SaPycTM;
DE            Short=SaPycTM {ECO:0000303|PubMed:34644530};
GN   Name=pycTM {ECO:0000303|PubMed:34644530};
GN   ORFNames=ERS179182_02233 {ECO:0000303|Ref.1};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSAR724;
RG   Pathogen Informatics;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROBABLE FUNCTION, AND CLASSIFICATION.
RC   STRAIN=BSAR724;
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 E Pycsar system. {ECO:0000305|PubMed:34644530}.
CC   -!- FUNCTION: The effector gene of a two-gene Pycsar system. Expression of
CC       this and adjacent SaPycC cytidylate cyclase (AC P0DV38) probably
CC       confers resistance to bacteriophage. The genes are probably only
CC       expressed in response to bacteriophage infection. Probably only
CC       responds to cCMP (produced by its cognate NTP cyclase), acts by
CC       impairing membrane integrity. {ECO:0000305|PubMed:34644530}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
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DR   EMBL; CSOZ01000027; CPM02516.1; -; Genomic_DNA.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR043760; DUF5706.
DR   Pfam; PF18967; DUF5706; 1.
PE   3: Inferred from homology;
KW   Antiviral defense; Cell membrane; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..158
FT                   /note="Pycsar effector protein SaPycTM"
FT                   /id="PRO_0000455232"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   158 AA;  18499 MW;  83858A6B8453FA83 CRC64;
     MKKDEYIKLH QSYLNEYIKF ADAKALAIIS INGFILNFNF SKRNIKFHNT EDIFNFTAFI
     LLIITIILAA FAVYPRTNNR SEKGIIFWDN INSMGEKEFI EKVKFEKEEE LLEKTIQQNY
     FLAKTASMKY SIIRKVFIIS ALGYSCLLFS SIFQIICS