CAPV_VIBCH
ID CAPV_VIBCH Reviewed; 355 AA.
AC Q9KVG8;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=cGAMP-activated phospholipase {ECO:0000303|PubMed:29891656};
DE EC=3.1.1.- {ECO:0000269|PubMed:29891656};
DE EC=3.1.1.32 {ECO:0000269|PubMed:30787435};
DE AltName: Full=3',3'-cGAMP receptor CapV {ECO:0000305|PubMed:29891656};
DE AltName: Full=Patatin-like phospholipase {ECO:0000303|PubMed:29891656};
GN Name=capV {ECO:0000303|PubMed:29891656, ECO:0000303|PubMed:30787435};
GN OrderedLocusNames=VC_0178 {ECO:0000312|EMBL:AAF93354.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF SER-62.
RX PubMed=29891656; DOI=10.1073/pnas.1801233115;
RA Severin G.B., Ramliden M.S., Hawver L.A., Wang K., Pell M.E.,
RA Kieninger A.K., Khataokar A., O'Hara B.J., Behrmann L.V., Neiditch M.B.,
RA Benning C., Waters C.M., Ng W.L.;
RT "Direct activation of a phospholipase by cyclic GMP-AMP in El Tor Vibrio
RT cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E6048-E6055(2018).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, NOMENCLATURE, AND
RP SIMILARITY.
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 [4]
RP ANTIVIRAL DEFENSE, AND OPERON STRUCTURE.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
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 [5]
RP ANTIVIRAL DEFENSE, AND OPERON STRUCTURE.
RC STRAIN=El Tor C6706;
RX PubMed=32544385; DOI=10.1016/j.cell.2020.05.019;
RA Lowey B., Whiteley A.T., Keszei A.F.A., Morehouse B.R., Antine S.P.,
RA Cabrera V.J., Kashin D., Schwede F., Mekalanos J.J., Shao S., Lee A.S.Y.,
RA Kranzusch P.J.;
RT "CBASS immunity uses CARF-related effectors to sense 3'-5' and 2'-5'-linked
RT cyclic oligonucleotide signals and protect bacteria from phage infection.";
RL Cell 182:38-49(2020).
RN [6]
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 (PubMed:29891656, PubMed:30787435). Thus, degrades
CC phosphatidylethanolamine (PE) and phosphatidylglycerol (PG), the major
CC phospholipids in the cell membrane of V.cholerae, releasing 16:1 and
CC 18:1 free fatty acids (PubMed:29891656). {ECO:0000269|PubMed:29891656,
CC ECO:0000269|PubMed:30787435}.
CC -!- FUNCTION: Protects E.coli against phage P1 and T2 infection. When the 4
CC gene operon capV-dncV-cap2-cap3 is introduced in E.coli MG1655 there is
CC about 100-fold protection against phages P1 and T2 (PubMed:31533127).
CC Protects E.coli against phage T2 infection. When the CBASS operon
CC (capV-dcnV-cap2-cap3) is introduced in E.coli MG1655 there is a more
CC than 10(3) decrease in the efficiency of T2 plaque formation. Protects
CC 100-fold against phage T5, offers no protection against T7
CC (PubMed:32544385). {ECO:0000269|PubMed:31533127,
CC ECO:0000269|PubMed:32544385}.
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 -!- 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:0000269|PubMed:29891656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60625;
CC Evidence={ECO:0000305|PubMed:29891656};
CC -!- ACTIVITY REGULATION: Phospholipase activity is specifically activated
CC upon 3',3'-cGAMP binding. Is not activated by the other cyclic
CC dinucleotides 3',3'-cUAMP, 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 (DncV).
CC {ECO:0000269|PubMed:29891656, ECO:0000269|PubMed:30787435}.
CC -!- INDUCTION: Part of the CBASS operon consisting of capV-dncV-cap2-cap3.
CC {ECO:0000305|PubMed:31533127}.
CC -!- DISRUPTION PHENOTYPE: Deletion of capV suppresses cGAMP-dependent
CC growth phenotypes resulting from overexpression of dncV.
CC {ECO:0000269|PubMed:29891656}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR EMBL; AE003852; AAF93354.1; -; Genomic_DNA.
DR PIR; E82354; E82354.
DR RefSeq; NP_229835.1; NC_002505.1.
DR RefSeq; WP_001133548.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KVG8; -.
DR SMR; Q9KVG8; -.
DR STRING; 243277.VC_0178; -.
DR DNASU; 2614189; -.
DR EnsemblBacteria; AAF93354; AAF93354; VC_0178.
DR GeneID; 57738918; -.
DR KEGG; vch:VC_0178; -.
DR PATRIC; fig|243277.26.peg.162; -.
DR eggNOG; COG3621; Bacteria.
DR HOGENOM; CLU_000288_144_9_6; -.
DR OMA; PTYFEPA; -.
DR BioCyc; VCHO:VC0178-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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;
KW Reference proteome.
FT CHAIN 1..355
FT /note="cGAMP-activated phospholipase"
FT /id="PRO_0000447706"
FT DOMAIN 17..214
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 21..26
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 60..64
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 201..203
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MUTAGEN 62
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29891656"
SQ SEQUENCE 355 AA; 39203 MW; 609242940AC121A9 CRC64;
MPNPPEYEHL KNQVRILSLN GGGARGLFTI SLLAEIERII EEKQGINGFK VGDYFDLITG
TSIGGILALG LAYGKSAREL EDVFRKQAGY IFPEQKYPRF FPVFRRRYRL ARGPLYDSKP
LAKTIASMVG EESTFNDLKC RVLIPTVNLS TGKPQFFKTP HNPEFHRDGR IKLIDAALAT
SAAPTYFAPH YCVDLDSYFA DGGLVANNPS FIGLHEVFRD MATDFPEAKV SDVKILNVGT
LGEEYSLSPS SLAGKSGYLG LWGMGERLVL SAMAANQELH KAMLLREFAT HDAIGNFVRL
DNNIPHEAAS DITLDNASAS SLSNLASRGR QLATEEFTKN KALADFFKVP ARKFK
