PYCC_PROTD
ID PYCC_PROTD Reviewed; 308 AA.
AC A0A4V2JTK3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Uridylate cyclase {ECO:0000303|PubMed:34644530};
DE EC=4.6.1.- {ECO:0000269|PubMed:34644530};
DE EC=4.6.1.2 {ECO:0000269|PubMed:34644530};
DE AltName: Full=Cyclic UMP synthase;
DE Short=cUMP synthase {ECO:0000303|PubMed:34644530};
DE AltName: Full=PtPycC {ECO:0000303|PubMed:34644530};
GN Name=pycC {ECO:0000303|PubMed:34644530};
GN ORFNames=ET996_01260 {ECO:0000303|Ref.1};
OS Propioniciclava tarda.
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Propioniciclava.
OX NCBI_TaxID=433330;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22130 / JCM 15804 / WR061;
RA Huptas C., Wenning M., Breitenwieser F., Doll E., Von Neubeck M.,
RA Busse H.-J., Scherer S.;
RT "Lactibacter flavus gen. nov., sp. nov., a novel bacterium of the family
RT Propionibacteriaceae isolated from raw milk and dairy products.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND CLASSIFICATION.
RC STRAIN=DSM 22130 / JCM 15804 / WR061;
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 D Pycsar system. {ECO:0000305|PubMed:34644530}.
CC -!- FUNCTION: The pyrimidine cyclase gene of a two-gene Pycsar system,
CC generates cyclic UMP (cUMP) from UTP as well as cGMP from GTP to a
CC lesser extent, has little to no activity on ATP or CTP
CC (PubMed:34644530). Expression of this and adjacent effector PtPycTM (AC
CC A0A4Q9KQH5) probably confers resistance to bacteriophage. The genes are
CC probably only expressed in response to bacteriophage infection
CC (Probable). {ECO:0000269|PubMed:34644530, ECO:0000305|PubMed:34644530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|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; SDMR01000001; TBT96321.1; -; Genomic_DNA.
DR Proteomes; UP000291933; Unassembled WGS sequence.
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; Reference proteome.
FT CHAIN 1..308
FT /note="Uridylate cyclase"
FT /id="PRO_0000455224"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
SQ SEQUENCE 308 AA; 34073 MW; 1FE4A803D78C2CC0 CRC64;
MSDEDLFLTA LLDSLGKEVN TVLNNSPIKV EEKDGDFKAE DIPSPSSDTW VKLPEVVAVV
CDLKGSTHLG TGKHDTSTAR IYKSGVEGAV RVFHEFGANF IDIQGDGGFG LFWGERAHER
ALCAGVTIRT FSEEFVERLE KRWPEGLPET GYKVGIHAAR TLVKRIGTKR EISEQEAVWA
GRPVNYAAKC AQSADRHQVI ITQAVWDKMK DNDFIAFSCD CGDGPTANLW TDVTVDRLPE
EDRDAVVLNS PWCKTCGPAF CEAIMAGEKK RDIPSAVRTG INRMKMQKAL EAKRLRDSSR
NSALRGVR
