ID   LEP4_LEGPN              Reviewed;         287 AA.
AC   O68433;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
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   Legionella pneumophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=130b / Wadsworth / Serogroup 1;
RX   PubMed=9529113; DOI=10.1128/iai.66.4.1776-1782.1998;
RA   Liles M.R., Viswanathan V.K., Cianciotto N.P.;
RT   "Identification and temperature regulation of Legionella pneumophila genes
RT   involved in type IV pilus biogenesis and type II protein secretion.";
RL   Infect. Immun. 66:1776-1782(1998).
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}.
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DR   EMBL; AF038655; AAC12718.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68433; -.
DR   STRING; 297246.lpp1481; -.
DR   TCDB; 3.A.15.3.1; the outer membrane protein secreting main terminal branch (mtb) family.
DR   eggNOG; COG1989; Bacteria.
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..287
FT                   /note="Prepilin leader peptidase/N-methyltransferase"
FT                   /id="PRO_0000192622"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P22610"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P22610"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P22610"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P22610"
SQ   SEQUENCE   287 AA;  32850 MW;  3DA1B1968498EB66 CRC64;
     MINALIINYP WFMYLVVGLF SLAVGSLLNV IIYRLPIILQ EEWKEQCCEL FHFEQRKEKI
     KLNLFLPRSF CPHCKAMVKA WQNIPLLAIL VLRGRCYQCD SPFSIRYPFV ETLTTVLSLY
     ASWHFGFTIQ LLFALLAIWI LISLVFIDLD HQLLPDSLTL GLLWIGLIAN TQNVFVSLDV
     AVLSCAGAYL ALWLFINLFY LMTCKVCMGH GDFKLFAAFG AWLGWMYLPI ILLISSITGA
     IIGLIYLKIN GKSRDTAIPF GPFLCISGLI AMFWGDSIIN WYIGYWM