CAPV_ECOLX
ID CAPV_ECOLX Reviewed; 356 AA.
AC P0DTE9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 25-MAY-2022, entry version 5.
DE RecName: Full=cGAMP-activated phospholipase {ECO:0000303|PubMed:31533127};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:Q6XGD4};
DE AltName: Full=3',3'-cGAMP receptor CapV;
DE AltName: Full=Patatin-like phospholipase;
GN Name=capV {ECO:0000303|PubMed:31533127}; ORFNames=ESG_RS0100140;
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=TW11681;
RX PubMed=21078854; DOI=10.1128/iai.00932-10;
RA Sahl J.W., Steinsland H., Redman J.C., Angiuoli S.V., Nataro J.P.,
RA Sommerfelt H., Rasko D.A.;
RT "A comparative genomic analysis of diverse clonal types of enterotoxigenic
RT Escherichia coli reveals pathovar-specific conservation.";
RL Infect. Immun. 79:950-960(2011).
RN [2]
RP FUNCTION AS A PHOSPHOLIPASE, ANTIVIRAL DEFENSE, NOMENCLATURE, OPERON
RP STRUCTURE, AND MUTAGENESIS OF SER-60.
RC STRAIN=TW11681;
RX PubMed=31533127; DOI=10.1038/s41586-019-1605-5;
RA Cohen D., Melamed S., Millman A., Shulman G., Oppenheimer-Shaanan Y.,
RA Kacen A., Doron S., Amitai G., Sorek R.;
RT "Cyclic GMP-AMP signalling protects bacteria against viral infection.";
RL Nature 574:691-695(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(GA) CBASS system (PubMed:32839535).
CC {ECO:0000269|PubMed:31533127, ECO:0000303|PubMed:32839535}.
CC -!- FUNCTION: Phospholipase that is activated upon binding to the cyclic
CC dinucleotide (CDN) second messenger 3',3'-cyclic GMP-AMP (3',3'-cGAMP).
CC {ECO:0000269|PubMed:31533127}.
CC -!- FUNCTION: Protects E.coli against phage infection. When capV and dncV
CC are introduced in E.coli MG1655 there is 1000-fold protection against
CC phage P1; protection against other phage (T2, T4, T5, T6 and lambda-
CC vir) requires the 2 subsequent genes (cap2 and cap3). Upon P1 phage
CC infection the activating molecule is produced between 30 and 40
CC minutes. Activation leads to bacterial cell lysis and death, which
CC occurs before the phage has finished its replication cycle, thus
CC protecting non-infected bacteria by aborting the phage infection and
CC preventing its propagation. {ECO:0000269|PubMed:31533127}.
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:0000250|UniProtKB:Q9KVG8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000250|UniProtKB:Q9KVG8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 2
CC H2O = 2 (9Z)-octadecenoate + 2 H(+) + sn-glycero-3-
CC phosphoethanolamine; Xref=Rhea:RHEA:60624, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74986,
CC ChEBI:CHEBI:143890; Evidence={ECO:0000250|UniProtKB:Q9KVG8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60625;
CC Evidence={ECO:0000250|UniProtKB:Q9KVG8};
CC -!- ACTIVITY REGULATION: Phospholipase activity is specifically activated
CC upon 3',3'-cGAMP binding, which is produced by the cognate cyclic
CC nucleotide synthase encoded in the same operon.
CC {ECO:0000269|PubMed:31533127}.
CC -!- INDUCTION: Part of the CBASS operon consisting of capV-dncV-cap2-cap3.
CC {ECO:0000305|PubMed:31533127}.
CC -!- MISCELLANEOUS: The sequence of this protein is available under the NCBI
CC RefSeq accession WP_001286317.1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR EMBL; AELD01000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_001286317.1; NZ_VTME01000123.1.
DR AlphaFoldDB; P0DTE9; -.
DR SMR; P0DTE9; -.
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..356
FT /note="cGAMP-activated phospholipase"
FT /id="PRO_0000451860"
FT DOMAIN 15..206
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 19..24
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 58..62
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 193..195
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MUTAGEN 60
FT /note="S->A: No longer defends against phage."
FT /evidence="ECO:0000269|PubMed:31533127"
SQ SEQUENCE 356 AA; 39562 MW; 1362F4B56D50CCDF CRC64;
MSDVSAVDKP RVRVLSLNGG GARGMFTISI LAEIERILAR KHPHQDIKIG DYFDLITGTS
IGGILALGLA TGKSARELES VFFDKAKDIF PTRWSLVNLC KALCAPIYNS SPLRETIEMM
IGAETTFNDL TRRVMIPAVN LSTGKPLFFK TPHNPDFTRD GPLKLIDAAL ATSAAPTYFA
PHYCKDLRSY FADGGLVANN PSYIGLLEVF RDMKSDFDVS HKDVYILNIG TVGEDYSLSP
SLLSKKRWTG YCHLWGMGKR LVLTTMTANQ HLHKNMLLRE LALHDALDNY LYLDEVIPNE
AASDITLDNA SDSSLQNLSA RGKQLANVQF AQNQKLKNFF ISPAKPFKRT DVQEKL
