PYCC_BURCE
ID PYCC_BURCE Reviewed; 229 AA.
AC A0A0J5ZXG5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Uridylate cyclase {ECO:0000303|PubMed:34644530};
DE EC=4.6.1.- {ECO:0000269|PubMed:34644530};
DE AltName: Full=BcPycC {ECO:0000303|PubMed:34644530};
DE AltName: Full=Cyclic UMP synthase {ECO:0000303|PubMed:34644530};
DE Short=cUMP synthase {ECO:0000303|PubMed:34644530};
GN Name=pycC {ECO:0000303|PubMed:34644530};
GN ORFNames=VL15_12785 {ECO:0000303|Ref.1};
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LK29;
RA Chan X.Y.;
RT "Draft genome of Burkholderia cepacia LK29.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:7R65}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 2-229, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CLASSIFICATION,
RP AND MUTAGENESIS OF TYR-50; ASP-52; ASP-94; ASP-96; ARG-97; ASN-172 AND
RP ASN-179.
RC STRAIN=LK29;
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 generates cyclic UMP (cUMP) from UTP, has little to no activity on ATP,
CC CTP or GTP (PubMed:34644530). Expression of this and adjacent effector
CC BcPycTIR (AC A0A0J5WTU0) probably confers resistance to bacteriophage.
CC The genes are probably only expressed in response to bacteriophage
CC 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:0000269|PubMed:34644530};
CC Note=Slightly more active with Mn(2+) than with Mg(2+).
CC {ECO:0000269|PubMed:34644530};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-9.5. {ECO:0000269|PubMed:34644530};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:34644530}.
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; LDWR01000021; KML58095.1; -; Genomic_DNA.
DR RefSeq; WP_048245919.1; NZ_LDWR01000021.1.
DR PDB; 7R65; X-ray; 1.45 A; A/B/C/D=2-229.
DR PDBsum; 7R65; -.
DR SMR; A0A0J5ZXG5; -.
DR EnsemblBacteria; KML58095; KML58095; VL15_12785.
DR PATRIC; fig|292.27.peg.2412; -.
DR Proteomes; UP000036338; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Lyase; Manganese;
KW Metal-binding; Nucleotide-binding.
FT CHAIN 1..229
FT /note="Uridylate cyclase"
FT /id="PRO_0000455221"
FT DOMAIN 47..178
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 50
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 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 52
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="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 96
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 97
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P0DV40,
FT ECO:0000305|PubMed:34644530"
FT MUTAGEN 50
FT /note="Y->A: Decreased cUMP production."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 52
FT /note="D->A: No cUMP production."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 94
FT /note="D->A: Decreased cUMP production."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 96
FT /note="D->A: No cUMP production."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 97
FT /note="R->A: Decreased cUMP production."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 172
FT /note="N->A: Almost no cUMP production."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 179
FT /note="N->A: Wild-type cUMP production."
FT /evidence="ECO:0000269|PubMed:34644530"
SQ SEQUENCE 229 AA; 25594 MW; E92430F69C61E752 CRC64;
MALADDLKKW VGETFTGKWE VQETTSVPNP EDLRLNSNHA KDLKAATVLY ADLDGSTDMV
NTKKWQFSAQ IYKTFLKCAS DIIRDEGGNI TAYDGDRVMA VFTGNSKNTS AARCALKINS
AVLDIIQPAI AKKWQTDFVL RHVVGIDTSQ LRTARIGIRG DNDLVWIGRA ANYAAKLTNL
AGKPTRITAD VYNKLADKLK YANGVDMWAP EHWDDMGIWT YTSTWKWTV
