ID   LEP4_DICCH              Reviewed;         283 AA.
AC   P31711;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Prepilin leader peptidase/N-methyltransferase;
DE   AltName: Full=Pectic enzymes secretion protein OutO;
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=outO;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC16;
RX   PubMed=1429461; DOI=10.1128/jb.174.22.7385-7397.1992;
RA   Lindeberg M., Collmer A.;
RT   "Analysis of eight out genes in a cluster required for pectic enzyme
RT   secretion by Erwinia chrysanthemi: sequence comparison with secretion genes
RT   from other Gram-negative bacteria.";
RL   J. Bacteriol. 174:7385-7397(1992).
CC   -!- FUNCTION: Plays a role in type II pseudopili formation by
CC       proteolytically removing the leader sequence from substrate proteins
CC       and subsequently monomethylating the alpha-amino group of the newly
CC       exposed N-terminal phenylalanine. Substrates include proteins required
CC       for biogenesis of the type II general secretory apparatus.
CC       {ECO:0000250|UniProtKB:P25960}.
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   -!- 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; L02214; AAA24841.1; -; Genomic_DNA.
DR   PIR; C47755; C47755.
DR   AlphaFoldDB; P31711; -.
DR   MEROPS; A24.A10; -.
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: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; Methyltransferase;
KW   Multifunctional enzyme; Protease; S-adenosyl-L-methionine; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..283
FT                   /note="Prepilin leader peptidase/N-methyltransferase"
FT                   /id="PRO_0000192620"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   283 AA;  31355 MW;  90B9CE722C4AAA7E CRC64;
     MDLIAFANTF PRVWLLALLL LGLIIGSFLN VVIYRLPLML ERSWRQEARF HLGLPAGRPL
     ARYDLCWPPS SCPHCHQRLR MRDNIPLLSW IWLRGRAHCC GGAVSWRYPL IELLSGLSFL
     LAGLLWQPGL ALLGALLCFG IFVALAAIDA RTQLLPDVMT LPLLWGGLLF NLADTFVPLE
     QAVVGAVAGY LSLWLIYWAF RLLSGREALG HGDFKLLAAL GAWLGWQALP NLVLIASLTG
     LTATLLWQRI HRLSMQQPLA FGPWLAVSGA MGLVLNVLGG WSH