ID   LEP4_PSEPU              Reviewed;         288 AA.
AC   P36642;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Prepilin leader peptidase/N-methyltransferase;
DE   AltName: Full=Protein PilD;
DE   AltName: Full=Protein secretion protein XCPA;
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; Synonyms=xcpA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCS358;
RX   PubMed=7905475; DOI=10.1128/jb.176.3.642-650.1994;
RA   de Groot A., Heijnen I., de Cock H., Filloux A., Tommassen J.;
RT   "Characterization of type IV pilus genes in plant growth-promoting
RT   Pseudomonas putida WCS358.";
RL   J. Bacteriol. 176:642-650(1994).
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; X74276; CAA52334.1; -; Genomic_DNA.
DR   PIR; B36961; B36961.
DR   AlphaFoldDB; P36642; -.
DR   MEROPS; A24.001; -.
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..288
FT                   /note="Prepilin leader peptidase/N-methyltransferase"
FT                   /id="PRO_0000192626"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
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        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
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   288 AA;  31972 MW;  CB7F63F85317F901 CRC64;
     MTLWTFLAME PAYFITLATV LGLLVGSFLN VVVYRLPIML ERQWQREAHE VLGLPVTEHE
     RFDLCLPASQ CTQCGHRIRA WENLPVLSYL ALRGRCSACK QRISVRYPLV EVGCALLSMV
     VAWRYGASVE ALVLLPLTWS LLALSLIDHD QQLLPDAIVL PGLWLGLIVN YFGVWVPLPD
     AVCGAVVGYL SLWTVYWLFK LVTGKEGMGY GDFKLLALLG AWGGWQVLPL TLLLSSVLGA
     LVGVYLLRVR NDSMGTAMPF GPYLAIAGWI AVLWGDEIYA SNMQLLGF