ID   LEP4_DICNO              Reviewed;         286 AA.
AC   Q46525;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=fimP;
OS   Dichelobacter nodosus (Bacteroides nodosus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A198;
RX   PubMed=7642131; DOI=10.1016/0378-1119(95)00264-7;
RA   Johnston J.L., Billington S.J., Haring V., Rood J.I.;
RT   "Identification of fimbrial assembly genes from Dichelobacter nodosus:
RT   evidence that fimP encodes the type-IV prepilin peptidase.";
RL   Gene 161:21-26(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}.
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DR   EMBL; U17138; AAB65807.1; -; Genomic_DNA.
DR   RefSeq; WP_012031428.1; NZ_SRJB01000012.1.
DR   AlphaFoldDB; Q46525; -.
DR   MEROPS; A24.001; -.
DR   PATRIC; fig|870.4.peg.1003; -.
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_0000192617"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P22610"
FT   BINDING         77
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"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P22610"
SQ   SEQUENCE   286 AA;  31863 MW;  6EF18DA03FC175DB CRC64;
     MLISELLQTP LGIFFVGLFS LMVGSFLNVV IYRVPVMMDR EEKQYAWQVF HGEDSVCPEI
     PKQRFNLLVP ASRCPHCGHR IRAIENIPVI SWLFLKGKCS GCGAAISARY LLVELLTAAL
     SVIVAFHYHD PLSLGFALVF TWTLIALCFI DAEHQLLPDR LTLPLLWLGI LAALFNVFIN
     LESSVIGAMI GYLSLWSVYW LFKLITGREG MGYGDFKLLA CLCAWQGAWM LPIILFSAAI
     LGMIYALGIG LRMGKPMPFG PFLAIAGWLT FLYGAQIGQL FGYFPA