PYCC_TREPO
ID PYCC_TREPO Reviewed; 286 AA.
AC A0A1T4LJ54;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
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=TpPycC {ECO:0000303|PubMed:34644530};
GN Name=pycC {ECO:0000303|PubMed:34644530};
GN ORFNames=SAMN02745149_01624 {ECO:0000303|Ref.1};
OS Treponema porcinum.
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=261392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-908 / CIP 108245 / JCM 2342 / 14V28;
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND CLASSIFICATION.
RC STRAIN=ATCC BAA-908 / CIP 108245 / JCM 2342 / 14V28;
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 TpPycTM (AC A0A1T4LJG1) 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; FUWG01000011; SJZ54745.1; -; Genomic_DNA.
DR STRING; 261392.SAMN02745149_01624; -.
DR EnsemblBacteria; SJZ54745; SJZ54745; SAMN02745149_01624.
DR Proteomes; UP000190423; 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 Antiviral defense; Cytoplasm; Lyase; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..286
FT /note="Uridylate cyclase"
FT /id="PRO_0000455228"
FT DOMAIN 90..223
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 93
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 95
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 95
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="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 140
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 140
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
SQ SEQUENCE 286 AA; 32645 MW; 1B570B8DD7ABAC23 CRC64;
MKNDNGQQLS LTQALDLLKS RQGKNFKTAD KIIENFCFYD YSNIIMKYDY KSGKKRILNI
LNSELDVENL NELPCDEKLT FSNAYYSWVT AIFVDIRKST ELFTNENKKD VSRLIRSFTS
EIIEIINQGD NLREIGIRGD CVYGIFTTPK KSQINEVFDM ACYVNTMIKM LNKLLIKEDI
PQIMVGIGVS SAQELVVKAG RKGSGVNNKV WIGDAVTKAA NMSGKGNKNH NLPIIISELT
YKNLNDHNKG LMSSRKYNDD LDYYYDCDLI ISAFNDWINK GMLDNE
