CAPE_ECOLX
ID CAPE_ECOLX Reviewed; 320 AA.
AC Q6XGD4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=cUMP-AMP-activated phospholipase {ECO:0000303|PubMed:30787435};
DE EC=3.1.1.32 {ECO:0000269|PubMed:30787435};
DE AltName: Full=3',3'-cUAMP receptor CapE {ECO:0000305|PubMed:30787435};
DE AltName: Full=Patatin-like phospholipase {ECO:0000303|PubMed:30787435};
GN Name=capE {ECO:0000303|PubMed:30787435};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35350 / ECOR 31;
RX PubMed=14731283; DOI=10.1046/j.1365-2958.2003.03870.x;
RA Schubert S., Dufke S., Sorsa J., Heesemann J.;
RT "A novel integrative and conjugative element (ICE) of Escherichia coli: the
RT putative progenitor of the Yersinia high-pathogenicity island.";
RL Mol. Microbiol. 51:837-848(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, NOMENCLATURE, AND
RP SIMILARITY.
RC STRAIN=ATCC 35350 / ECOR 31;
RX PubMed=30787435; DOI=10.1038/s41586-019-0953-5;
RA Whiteley A.T., Eaglesham J.B., de Oliveira Mann C.C., Morehouse B.R.,
RA Lowey B., Nieminen E.A., Danilchanka O., King D.S., Lee A.S.Y.,
RA Mekalanos J.J., Kranzusch P.J.;
RT "Bacterial cGAS-like enzymes synthesize diverse nucleotide signals.";
RL Nature 567:194-199(2019).
RN [3]
RP CLASSIFICATION AND NOMENCLATURE.
RX PubMed=32839535; DOI=10.1038/s41564-020-0777-y;
RA Millman A., Melamed S., Amitai G., Sorek R.;
RT "Diversity and classification of cyclic-oligonucleotide-based anti-phage
RT signalling systems.";
RL Nat. Microbiol. 5:1608-1615(2020).
CC -!- FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling
CC system) provides immunity against bacteriophage. The CD-NTase protein
CC synthesizes cyclic nucleotides in response to infection; these serve as
CC specific second messenger signals. The signals activate a diverse range
CC of effectors, leading to bacterial cell death and thus abortive phage
CC infection. A type II-A(UA) CBASS system (PubMed:32839535).
CC {ECO:0000303|PubMed:32839535, ECO:0000305}.
CC -!- FUNCTION: Phospholipase that is activated upon binding to the cyclic
CC dinucleotide (CDN) second messenger 3',3'-cyclic UMP-AMP (3',3'-cUAMP).
CC {ECO:0000269|PubMed:30787435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:30787435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000305|PubMed:30787435};
CC -!- ACTIVITY REGULATION: Phospholipase activity is specifically activated
CC upon 3',3'-cUAMP binding. Is not activated by the other cyclic
CC dinucleotides 3',3'-cGAMP, 3',3'-c-diAMP and 3',3'-c-diGMP. Therefore,
CC is specifically activated by only the nucleotide synthesized from its
CC adjacently encoded nucleotidyltransferase (CdnE).
CC {ECO:0000269|PubMed:30787435}.
CC -!- MISCELLANEOUS: This is a complex CBASS locus with the loci capE-cdnE-
CC probable diadenylate cyclase-capV-dcnV1-cap2-cap3.
CC {ECO:0000305|PubMed:14731283}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP70300.1; Type=Frameshift; Evidence={ECO:0000305};
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; AY233333; AAP70300.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; WP_001593459.1; NZ_VTMJ01000059.1.
DR AlphaFoldDB; Q6XGD4; -.
DR SMR; Q6XGD4; -.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Hydrolase; Lipid degradation; Lipid metabolism.
FT CHAIN 1..320
FT /note="cUMP-AMP-activated phospholipase"
FT /id="PRO_0000447707"
FT DOMAIN 23..204
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 27..32
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 59..63
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 191..193
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 61
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 320 AA; 35366 MW; F0C5E6821E8FEE91 CRC64;
MTYSVSPSSL LTEYGNDNIC RVLALDGGGA KGFYTLGVLK EIEAMLGCPL YKRFDLVFGT
STGAIIAALI ALGYEVDQIH ALYTEHVPRV MSSRSAAART MALQDLAKEV FQDKTFEDVL
MGIGIVATRW MTERPMIFKG NVVQAHGRKG TFSPGFGVSI ADAVQASCSA YPFFERKVIV
TAAGDKVELI DGGYCANNPT LFAIADATVA LKKDHKDIRV INVGVGIYPE PKPGLLMRIA
KKWLAVQLLQ KTLEINTQSM DQLRDILFKD IPTIRISDTF ERPEMATDLL EYNLDKLNTL
RQRGRESFGA REAQLREFLI
