MONAL_PSEE4
ID MONAL_PSEE4 Reviewed; 271 AA.
AC Q1I8U1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Monalysin {ECO:0000303|PubMed:21980286};
DE AltName: Full=beta-barrel pore-forming toxin {ECO:0000303|PubMed:25847242};
DE Short=beta-PFT {ECO:0000303|PubMed:25847242};
DE Flags: Precursor;
GN Name=mnl {ECO:0000303|PubMed:21980286};
GN OrderedLocusNames=PSEEN3174 {ECO:0000312|EMBL:CAK15937.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
RN [2]
RP PROTEIN SEQUENCE OF 34-39, FUNCTION, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, N-TERMINAL PROCESSING, SUBUNIT, AND INDUCTION.
RC STRAIN=L48;
RX PubMed=21980286; DOI=10.1371/journal.ppat.1002259;
RA Opota O., Vallet-Gely I., Vincentelli R., Kellenberger C., Iacovache I.,
RA Gonzalez M.R., Roussel A., van der Goot F.G., Lemaitre B.;
RT "Monalysin, a novel beta-pore-forming toxin from the Drosophila pathogen
RT Pseudomonas entomophila, contributes to host intestinal damage and
RT lethality.";
RL PLoS Pathog. 7:E1002259-E1002259(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 9-271 OF THE PRO-FORM OF
RP MONALYSIN; THE CLEAVED FORM AND AN INACTIVE MUTANT LACKING THE
RP MEMBRANE-SPANNING REGION, SUBUNIT, AND DOMAIN.
RC STRAIN=L48;
RX PubMed=25847242; DOI=10.1074/jbc.m115.646109;
RA Leone P., Bebeacua C., Opota O., Kellenberger C., Klaholz B., Orlov I.,
RA Cambillau C., Lemaitre B., Roussel A.;
RT "X-ray and cryo-electron microscopy structures of Monalysin pore-forming
RT toxin reveal multimerization of the pro-form.";
RL J. Biol. Chem. 290:13191-13201(2015).
CC -!- FUNCTION: Pore-forming toxin that contributes to the virulence of
CC P.entomophila against Drosophila, playing an important role in host
CC intestinal damage and lethality. Displays cytolytic and hemolytic
CC activity. {ECO:0000269|PubMed:21980286}.
CC -!- SUBUNIT: Pro-Monalysin forms a stable donut-like 18-mer complex
CC composed of two disk-shaped nonamers held together by N-terminal
CC swapping of the pro-peptides (PubMed:25847242). After proteolytic
CC cleavage, the inactive 18-mer complex probably dissociates into two
CC disk-shaped active nonamers in which the transmembrane segments are
CC unmasked and ready to engage the conformational change leading to the
CC pore formation into the target membrane (PubMed:25847242). Multimerizes
CC into circular-like structures and barrel-like aggregates
CC (PubMed:21980286). {ECO:0000269|PubMed:21980286,
CC ECO:0000269|PubMed:25847242}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21980286}. Host cell
CC membrane {ECO:0000305|PubMed:21980286}.
CC -!- INDUCTION: Is regulated by both the GacS/GacA two-component system and
CC the Pvf regulator, two signaling systems that control P.entomophila
CC pathogenicity. {ECO:0000269|PubMed:21980286}.
CC -!- DOMAIN: Monalysin structure belongs to the Aerolysin-like PFTs fold
CC family but is devoid of obvious receptor-binding domain.
CC {ECO:0000305|PubMed:25847242}.
CC -!- PTM: Requires N-terminal cleavage to become fully active. The
CC metalloprotease AprA can induce the rapid cleavage of pro-Monalysin
CC into its active form. Can also be processed by trypsin.
CC {ECO:0000269|PubMed:21980286}.
CC -!- DISRUPTION PHENOTYPE: Reduced cell death is observed upon infection
CC with a mutant deficient in Monalysin production. This mutant is
CC affected in its abilities to induce cell damage in the Drosophila gut.
CC It induces lower level of stress and repair pathway activity than wild-
CC type. {ECO:0000269|PubMed:21980286}.
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DR EMBL; CT573326; CAK15937.1; -; Genomic_DNA.
DR RefSeq; WP_011534324.1; NC_008027.1.
DR PDB; 4MJT; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I=36-271, J/K/L/M/N/O/P/Q/R=9-35.
DR PDB; 4MKO; X-ray; 1.70 A; A/B/C/D=36-271.
DR PDB; 4MKQ; X-ray; 2.65 A; A/B=36-101, A/B=171-271, C/D=9-35.
DR PDBsum; 4MJT; -.
DR PDBsum; 4MKO; -.
DR PDBsum; 4MKQ; -.
DR AlphaFoldDB; Q1I8U1; -.
DR SMR; Q1I8U1; -.
DR TCDB; 1.C.59.3.1; the clostridium perfringens enterotoxin (cpe) family.
DR EnsemblBacteria; CAK15937; CAK15937; PSEEN3174.
DR KEGG; pen:PSEEN3174; -.
DR eggNOG; ENOG5034BB4; Bacteria.
DR HOGENOM; CLU_1160292_0_0_6; -.
DR OMA; YNDPHRR; -.
DR OrthoDB; 1932623at2; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IDA:UniProtKB.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR InterPro; IPR040927; BB_PF.
DR Pfam; PF18063; BB_PF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Hemolysis;
KW Host cell membrane; Host membrane; Ion transport; Membrane; Porin;
KW Secreted; Toxin; Transmembrane; Transmembrane beta strand; Transport;
KW Virulence; Zymogen.
FT PROPEP 1..33
FT /evidence="ECO:0000269|PubMed:21980286"
FT /id="PRO_0000439889"
FT CHAIN 34..271
FT /note="Monalysin"
FT /id="PRO_0000439890"
FT REGION 102..170
FT /note="Pore-forming domain"
FT /evidence="ECO:0000305|PubMed:25847242"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4MKO"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4MKQ"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 81..102
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 107..118
FT /evidence="ECO:0007829|PDB:4MKO"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4MJT"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4MKO"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:4MKO"
FT TURN 151..155
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 159..186
FT /evidence="ECO:0007829|PDB:4MKO"
FT TURN 187..192
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 208..226
FT /evidence="ECO:0007829|PDB:4MKO"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4MKO"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:4MKO"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:4MKO"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:4MKO"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4MKO"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:4MKO"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4MKO"
SQ SEQUENCE 271 AA; 30201 MW; D421D694A7DBACB7 CRC64;
MTIKEELGQP QSHSIELDEV SKEAASTRAA LTSNLSGRFD QYPTKKGDFA IDGYLLDYSS
PKQGCWVDGI TVYGDIYIGK QNWGTYTRPV FAYLQYVETI SIPQNVTTTL SYQLTKGHTR
SFETSVNAKY SVGANIDIVN VGSEISTGFT RSESWSTTQS FTDTTEMKGP GTFVIYQVVL
VYAHNATSAG RQNANAFAYS KTQAVGSRVD LYYLSAITQR KRVIVPSSNA VTPLDWDTVQ
RNVLMENYNP GSNSGHFSFD WSAYNDPHRR Y
