PYCC_RHOS2
ID PYCC_RHOS2 Reviewed; 240 AA.
AC A0A1V0HUX5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Uridylate cyclase {ECO:0000303|PubMed:34644530};
DE EC=4.6.1.- {ECO:0000269|PubMed:34644530};
DE AltName: Full=Cyclic UMP synthase;
DE Short=cUMP synthase {ECO:0000303|PubMed:34644530};
DE AltName: Full=RsmPycC {ECO:0000303|PubMed:34644530};
GN Name=pycC {ECO:0000303|PubMed:34644530};
GN ORFNames=B5V46_03430 {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 FUNCTION, CATALYTIC ACTIVITY, 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 pyrimidine cyclase gene of a two-gene Pycsar system,
CC weakly generates cyclic UMP (cUMP) from UTP, has little to no activity
CC on ATP, CTP or GTP (PubMed:34644530). Expression of this and adjacent
CC effector RsmPycTM (AC A0A1V0HUU2) probably confers resistance to
CC bacteriophage. The genes are probably only expressed in response to
CC bacteriophage infection (Probable). {ECO:0000269|PubMed:34644530,
CC 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 -!- 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; CP020384; ARC87741.1; -; Genomic_DNA.
DR STRING; 308754.B5V46_03430; -.
DR EnsemblBacteria; ARC87741; ARC87741; B5V46_03430.
DR KEGG; rhm:B5V46_03430; -.
DR Proteomes; UP000191232; Chromosome.
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 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Lyase; Manganese; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..240
FT /note="Uridylate cyclase"
FT /id="PRO_0000455227"
FT DOMAIN 45..180
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 48
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 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 94
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 94
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="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P0DV40,
FT ECO:0000305|PubMed:34644530"
SQ SEQUENCE 240 AA; 26685 MW; B52C3AF43A8E8129 CRC64;
MSINDDISSD VMRIRDADWN KRSGSKVPSP GDVTLSNGAV EIDATYLYAD MANSSRMAKE
LDRRVTAKIL KSFLASSSRL ISHFGGTIMS FDGDRVMGAF MGDAKNSSAI KCSFSIAYSV
TQLIRPKFES KYDTVKNAGF KIRHATGVDT GTVFVVRGGI YGSNELISIG RAPNLAAKLS
DLREGEYTTF ATKSVYDRTN KLQKQRLDGS SDIWEKRDWD FCDENITIYR SSYWRKPGSN
