ID   PYCC_GULMO              Reviewed;         258 AA.
AC   P0DV42;
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:0000269|PubMed:34644530};
DE   AltName: Full=Cyclic UMP synthase;
DE            Short=cUMP synthase {ECO:0000303|PubMed:34644530};
DE   AltName: Full=GmPycC {ECO:0000303|PubMed:34644530};
GN   Name=pycC {ECO:0000303|PubMed:34644530};
GN   ORFNames=Ga0100804_10533 {ECO:0000303|PubMed:26586874};
OS   Gulbenkiania mobilis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Gulbenkiania.
OX   NCBI_TaxID=397457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB1;
RX   PubMed=26586874; DOI=10.1128/genomea.01295-15;
RA   Saxena R., Chaudhary N., Dhakan D.B., Sharma V.K.;
RT   "Draft Genome Sequence of Gulbenkiania mobilis Strain MB1, a Sulfur-
RT   Metabolizing Thermophile Isolated from a Hot Spring in Central India.";
RL   Genome Announc. 3:0-0(2015).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CLASSIFICATION.
RC   STRAIN=MB1;
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 C 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 GmPycTM (AC P0DV43) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LIVN01000053; -; NOT_ANNOTATED_CDS; 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   CDD; cd07302; CHD; 1.
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   Antiviral defense; Cytoplasm; Lyase; Manganese; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..258
FT                   /note="Uridylate cyclase"
FT                   /id="PRO_0000455222"
FT   DOMAIN          50..190
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         53
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         55
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:34644530"
FT   BINDING         55
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305|PubMed:34644530"
FT   BINDING         102
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:34644530"
FT   BINDING         102
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305|PubMed:34644530"
SQ   SEQUENCE   258 AA;  28778 MW;  DABC23BB78411554 CRC64;
     MRSSHKSFDF ENSLKRIDSI LNDSTSYEES DDIPDIDDLT FNNGKYVNCA AIFIDLRGST
     DLIKTLGKLS KSLARLYRAY ISEMVAIVNS FKTCKEINIV GDCVSAMFAG DIEGAESPVI
     EALQASSMAN AMMNVLNVKY KKKWKDFVEL KAGIGVAYGR ALVIKAGFSG SGIKDLVYMG
     DVVNKASKMC GLAYKEYTSH AICVTKEVYE NAGKYIANEE KKLTYQDFLT EKNHNTFGSV
     YVGNFHRVYI NNWAEENK