ID   LEP4_KLEPN              Reviewed;         228 AA.
AC   P15754;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Prepilin leader peptidase/N-methyltransferase;
DE   AltName: Full=Pullulanase secretion protein PulO;
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=pulO;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UNF 5023;
RX   PubMed=2162463; DOI=10.1111/j.1365-2958.1990.tb00604.x;
RA   Pugsley A.P., Reyss I.;
RT   "Five genes at the 3' end of the Klebsiella pneumoniae pulC operon are
RT   required for pullulanase secretion.";
RL   Mol. Microbiol. 4:365-379(1990).
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   -!- 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; M32613; AAA25137.1; -; Genomic_DNA.
DR   EMBL; X52462; CAA36700.1; -; Genomic_DNA.
DR   PIR; S11803; S11803.
DR   AlphaFoldDB; P15754; -.
DR   MEROPS; A24.A10; -.
DR   TCDB; 3.A.15.1.1; the outer membrane protein secreting main terminal branch (mtb) family.
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..228
FT                   /note="Prepilin leader peptidase/N-methyltransferase"
FT                   /id="PRO_0000192621"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   228 AA;  24754 MW;  38D5EE1A9E3BC7B8 CRC64;
     MVENIALLPE FAAQYPFLWG SFLFLSGLAF GSFFNVVIHR LPLMMEQAEG INLCFPASFC
     PQCREPIAWR DNIPLLGFLF LKGRSRCCGQ PISPRYPLME LATGALFVLA GYLMAPGVPL
     LGGLILLSLL LILAAIDAQT QLLPDGLTLP LMWAGLLFNL SATYVPLAEA VVGAMAGYLS
     LWSVYWVFRL LSGKEALGYG DFKLLAALGA WLGWQALPQT LLLASPAA