LEP4_VIBVU
ID LEP4_VIBVU Reviewed; 289 AA.
AC Q56740;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Prepilin leader peptidase/N-methyltransferase;
DE Includes:
DE RecName: Full=Leader peptidase;
DE EC=3.4.23.43 {ECO:0000250|UniProtKB:P22610};
DE AltName: Full=Prepilin peptidase;
DE Includes:
DE RecName: Full=N-methyltransferase;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P22610};
GN Name=vvpD; OrderedLocusNames=VV1_1623;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MO6-24;
RA Strom M.S., Lara J.C.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C7184;
RX PubMed=9826339; DOI=10.1128/iai.66.12.5659-5668.1998;
RA Paranjpye R.N., Lara J.C., Pepe J.C., Pepe C.M., Strom M.S.;
RT "The type IV leader peptidase/N-methyltransferase of Vibrio vulnificus
RT controls factors required for adherence to HEp-2 cells and virulence in
RT iron-overloaded mice.";
RL Infect. Immun. 66:5659-5668(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18604505; DOI=10.1007/s12275-008-0058-6;
RA Park J., Ryu S.Y., Kim C.M., Shin S.H.;
RT "Two forms of Vibrio vulnificus metalloprotease VvpE are secreted via the
RT type II general secretion system.";
RL J. Microbiol. 46:338-343(2008).
CC -!- FUNCTION: Plays an essential role in type IV pili and type II
CC pseudopili formation by proteolytically removing the leader sequence
CC from substrate proteins and subsequently monomethylating the alpha-
CC amino group of the newly exposed N-terminal phenylalanine.
CC {ECO:0000250|UniProtKB:P22610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-terminal,
CC basic peptide of 5-8 residues from type IV prepilin, and then N-
CC methylates the new N-terminal amino group, the methyl donor being S-
CC adenosyl-L-methionine.; EC=3.4.23.43;
CC Evidence={ECO:0000250|UniProtKB:P22610};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P22610};
CC Note=Zinc is required for the N-terminal methylation of the mature
CC pilin, but not for signal peptide cleavage.
CC {ECO:0000250|UniProtKB:P22610};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P22610}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P22610}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants are unable to secrete several
CC extracellular degradative enzymes including the cytolysin/hemolysin
CC tthat remains in the periplasmic space (PubMed:18604505). It results
CC also in significant decreases in host cell cytotoxicity, adherence and
CC virulence in a mouse mode (PubMed:9826339).
CC {ECO:0000269|PubMed:18604505, ECO:0000269|PubMed:9826339}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family. {ECO:0000305}.
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DR EMBL; U48808; AAA91206.1; -; Genomic_DNA.
DR EMBL; AF070934; AAC23601.1; -; Genomic_DNA.
DR EMBL; AE016795; AAO10042.1; -; Genomic_DNA.
DR RefSeq; WP_011079548.1; NC_004459.3.
DR AlphaFoldDB; Q56740; -.
DR MEROPS; A24.001; -.
DR EnsemblBacteria; AAO10042; AAO10042; VV1_1623.
DR KEGG; vvu:VV1_1623; -.
DR HOGENOM; CLU_057101_0_0_6; -.
DR OMA; VFWLFKL; -.
DR Proteomes; UP000002275; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR010627; Pept_A24A_N.
DR InterPro; IPR014032; Peptidase_A24A_bac.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR Pfam; PF06750; DiS_P_DiS; 1.
DR Pfam; PF01478; Peptidase_A24; 1.
DR PRINTS; PR00864; PREPILNPTASE.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Methyltransferase; Multifunctional enzyme; Protease;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..289
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000192630"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
SQ SEQUENCE 289 AA; 32295 MW; 0B3479B870F9C6B0 CRC64;
MDALQYYPWL YIGLASLFGL LVGSFLNVVI YRLPKIMELE WRQECAESFP EYNITPPTET
LTLSTPRSSC PSCHTPIRVR DNIPVFSWLA LRGKCHHCQT KISARYPFVE ALSAFLCGLV
AWKFGYAPIT VALIGFTLVL IAATFIDLDT MLLPDQLTLP LTWTGIALAL LEISPVSLQD
SVFGAMAGYL CLWSVYHLFR LLTGKEGMGY GDFKLLAALG AWLGWQYLPM IILLSSVVGL
IFGLIQLRLQ KQGIEMAFPF GPYLAIAGWV ALMWGDSLMS WYLNYLIGA
