PYCC_STAAU
ID PYCC_STAAU Reviewed; 423 AA.
AC P0DV38;
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=Cytidylate cyclase {ECO:0000303|PubMed:34644530};
DE EC=4.6.1.6 {ECO:0000269|PubMed:34644530};
DE AltName: Full=Cyclic CMP synthase;
DE Short=cCMP synthase {ECO:0000303|PubMed:34644530};
DE AltName: Full=SaPycC {ECO:0000303|PubMed:34644530};
GN Name=pycC {ECO:0000303|PubMed:34644530};
GN ORFNames=ERS179182_02234 {ECO:0000303|Ref.1};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSAR724;
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND CLASSIFICATION.
RC STRAIN=BSAR724;
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 E Pycsar system. {ECO:0000305|PubMed:34644530}.
CC -!- FUNCTION: The pyrimidine cyclase gene of a two-gene Pycsar system,
CC weakly generates cyclic CMP (cCMP) from CTP, has little to no activity
CC on ATP, GTP or UTP (PubMed:34644530). Expression of this and adjacent
CC effector SaPycTM (AC P0DV39) 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=CTP = 3',5'-cyclic CMP + diphosphate; Xref=Rhea:RHEA:14737,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58003; EC=4.6.1.6;
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 -!- DOMAIN: Has an N-terminal nucleotide cyclase domain and a C-terminal
CC nucleotide sensor domain (AGS-C). {ECO:0000305|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; CSOZ01000027; CPM02544.1; -; 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 CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR040511; AGS_C.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF18134; AGS_C; 1.
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..423
FT /note="Cytidylate cyclase"
FT /id="PRO_0000455220"
FT DOMAIN 79..184
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 290..409
FT /note="AGS-C domain"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 82
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 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
SQ SEQUENCE 423 AA; 49616 MW; FF2130855E5CDCC2 CRC64;
MVNHIRIFDN LFQSNISKFQ NLTSKSYIIR NDNEKNSYLP MVQEIRELFG KEGEIFSKSI
GTHPDFFGIE NTNEYQYICS LFVDISGSTK LALKYSLDKV KLYKNAIISS AIEIFRAFDG
HIHRIQGDAV LVYFGHKELE KSDAIINAIN AASLMQYFNA TTLKKFFESE NLEPLKIRIG
IDFGDDSSVL WSKYGIDGIN EITSTSIHTD LASKFQNKAP SNKIMIGENI NKYLDIPKKF
RSIKIEKNNG VDVEKRYILN TNNLGRYSME VFEWEKYLNS FSMLPPFSTE NEQFYSPRDL
KIRCWIIDEK NQDKYEYIER GSALKKEMNL LFKLEIYNQC LEFKNIKWRV VNYGEEAKKD
KELEFEMNQY EGYQYCNQKT AYTGLHFMEC YLYDINDKII CHDSFGLFIN DNNREVRKLG
IED
