PYCC2_ECOLX
ID PYCC2_ECOLX Reviewed; 463 AA.
AC P0DV26;
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=Ec303145PycC {ECO:0000303|PubMed:34644530};
GN Name=pycC {ECO:0000303|PubMed:34644530}; ORFNames=Ga0100619_101298;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=303145;
RA Hazen T.H., Donnenberg M., Nataro J., Kaper J., Rasko D.;
RT "Emergence of novel diverse phylogenomic lineages of EPEC.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ANTIVIRAL DEFENSE, AND CLASSIFICATION.
RC STRAIN=303145;
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:0000269|PubMed:34644530}.
CC -!- FUNCTION: The pyrimidine cyclase gene of a two-gene Pycsar system,
CC generates cyclic CMP (cCMP) from CTP in response to bacteriophage
CC infection. Has little to no activity on ATP, GTP or UTP
CC (PubMed:34644530). Expression of this and adjacent effector
CC Ec303145PycTM (AC P0DV27) confers resistance to bacteriophage P1, T5,
CC lambda-vir and phi27 (PubMed:34644530). {ECO:0000269|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; JHSG01000012; -; 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; 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..463
FT /note="Cytidylate cyclase"
FT /id="PRO_0000455219"
FT DOMAIN 122..231
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 334..454
FT /note="AGS-C domain"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 125
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 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 127
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="2"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:34644530"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:34644530"
SQ SEQUENCE 463 AA; 52991 MW; 76324EA0C83AA4A0 CRC64;
MSIKNLYKNL NDEMGSISKR RKNNNISFNK STFDSHAMDA LNTSFENYED ISLEGFESYI
NESASRTVIE RNSLVPLKDY DAVHSLRNAF GKPPRDNEPR IGTHPEFKHL ELDNRTDTGY
VVTMFMDIIG STKLGLSYSP SDVFLFKNNI ITGAIETINA FDGHVHRIMG DAVMAFFRSR
QNEQHDTLEN SVIDAINCAA YFIEVMNEIV KPQIKEVADE NIGIRIGIDL GETNYVLWGN
YGIPGVNEVT ATSFFVDIAS KLQHKAPKNS IMLGQNLVEK LGLTVNDYLT YKLKDGQPDR
YIIDFTSKNQ SRLRYKQYLL NQSKYFSILP HGLKPSRIKV VISYSNDELG LVNRKDYFNC
SSVIPKGKWV KFHATFCEEY GEHYESLKFK FRVVNNGLDA SKKDNYDNHE TEIIKKAYEK
ENGVFTAIHK EQTSYKGLQH MYISVISNDT VIEREIPCSI FIK
