PYCC_XANPE
ID PYCC_XANPE Reviewed; 231 AA.
AC P0DV28;
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=Uridylate cyclase {ECO:0000303|PubMed:34644530};
DE EC=4.6.1.- {ECO:0000305|PubMed:34644530};
DE AltName: Full=Cyclic UMP synthase;
DE Short=cUMP synthase {ECO:0000303|PubMed:34644530};
DE AltName: Full=XpPycC {ECO:0000303|PubMed:34644530};
GN Name=pycC {ECO:0000303|PubMed:34644530};
GN ORFNames=GEV1001_09735 {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, ANTIVIRAL DEFENSE, INDUCTION, AND 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 signal activates 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 pyrimidine cyclase gene of a two-gene Pycsar system,
CC generates cyclic UMP (cUMP) from UTP probably in response to
CC bacteriophage infection (Probable). Expression of this and adjacent
CC effector XpPycTIR (AC P0DV29) confers resistance to bacteriophage T7.
CC When cells expressing the Pycsar system are infected phage T7 at low
CC multiplicity of infection (0.2 MOI) the culture survives, at 2.0 MOI
CC bacteria enter growth arrest. The same cells enter growth arrest after
CC exposure to 2.5 mM cUMP but not cCMP; the effector protein responds
CC only to the cUMP produced by its cognate NTP cyclase (PubMed:34644530).
CC {ECO:0000269|PubMed:34644530, ECO:0000305|PubMed:34644530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UTP = 3',5'-cyclic UMP + diphosphate; Xref=Rhea:RHEA:69603,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:184387;
CC Evidence={ECO:0000269|PubMed:34644530};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0DV24};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0J5ZXG5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expression is probably induced by infection with phage T7.
CC {ECO:0000269|PubMed:34644530}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. Pyrimidine cyclase subfamily. {ECO:0000305|PubMed:34644530}.
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DR EMBL; JZVV01000016; KLD05781.1; -; Genomic_DNA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR SUPFAM; SSF55073; SSF55073; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cytoplasm; Lyase; Manganese; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..231
FT /note="Uridylate cyclase"
FT /id="PRO_0000455229"
FT DOMAIN 46..178
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 49
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P0DV40,
FT ECO:0000305|PubMed:34644530"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 95
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 95
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 96
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P0DV40,
FT ECO:0000305|PubMed:34644530"
SQ SEQUENCE 231 AA; 25965 MW; 475498989417580C CRC64;
MGLKDELTTF CHDVFNGNWE TTEGKNVPDE DSRLTLKNTA ITIDGTVLYA DLDGSTAMVD
GYKNWFAAEI YKTYLYCCAR IIAAEGGVVT AYDGDRVMAL FIGERKNTRA ARAAMKIKWA
VDEIIMPKKD ARYTSNKFAL KHVTGIDTCS LFVAKTGARG ANDLVWVGRA ANYAAKLTSL
PSTYTYITES VYKMLADEAK TSNGKSMWEK VTWNTFNNST IYRSNWRWRI D
