LEP4_NEIGO
ID LEP4_NEIGO Reviewed; 286 AA.
AC P33566; Q50963; Q53404;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=pilD;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MS11;
RX PubMed=8100347; DOI=10.1111/j.1365-2958.1993.tb01579.x;
RA Lauer P., Albertson N.H., Koomey M.;
RT "Conservation of genes encoding components of a type IV pilus assembly/two-
RT step protein export pathway in Neisseria gonorrhoeae.";
RL Mol. Microbiol. 8:357-368(1993).
RN [2]
RP SEQUENCE REVISION TO 247-255.
RA Koomey M.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MS11;
RX PubMed=7906688; DOI=10.1128/jb.176.5.1323-1331.1994;
RA Dupuy B., Pugsley A.P.;
RT "Type IV prepilin peptidase gene of Neisseria gonorrhoeae MS11: presence of
RT a related gene in other piliated and nonpiliated Neisseria strains.";
RL J. Bacteriol. 176:1323-1331(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-286.
RC STRAIN=MS11;
RX PubMed=7565116; DOI=10.1111/j.1365-2958.1995.tb02420.x;
RA Freitag N.E., Seifert H.S., Koomey M.;
RT "Characterization of the pilF-pilD pilus-assembly locus of Neisseria
RT gonorrhoeae.";
RL Mol. Microbiol. 16:575-586(1995).
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 -!- SIMILARITY: Belongs to the peptidase A24 family. {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; U32588; AAC43468.1; -; Genomic_DNA.
DR EMBL; S69067; AAB30050.1; -; Genomic_DNA.
DR PIR; A53374; A53374.
DR PIR; S32915; S32915.
DR RefSeq; WP_003689814.1; NZ_WHPL01000002.1.
DR AlphaFoldDB; P33566; -.
DR GeneID; 66753950; -.
DR OMA; VFWLFKL; -.
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..286
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000192624"
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 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
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"
FT CONFLICT 148
FT /note="A -> E (in Ref. 3; AAB30050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 31332 MW; A2941E7EDCACE275 CRC64;
MSDLSVLSPF AVPLAAVLGL LVGSFLNVVI YRVPVMMERG WTVFAKEHLN LPLTDDESRT
FNLMKPDSCC PKCRVPIRAW QNIPIVSYLL LRGKCASCQT KISIRYPLIE LLTGVLFGLV
AWQYGWSWIT LGGLILTAFL ISLTFIDADT QYLPDSMTLP LIWLGLIFNL DGGFVPLQSA
VLGAVAGYSS LWLLCAVYKL LTGKTGMGNG DFKLIAALGA WLGISALPVL IFVSSLIGLV
AAIVMRVAKG RHFAFGPALT VSGWIIFTAN DSVWRAVNWW LTHPVR
