LEP4_AERS4
ID LEP4_AERS4 Reviewed; 291 AA.
AC A2T195; O54483; O68964;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=tapD; Synonyms=pilD; OrderedLocusNames=ASA_0411;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lutwyche P., Perez-Casal J.F., Crump E.M., Trust T.J.;
RT "Aeromonas salmonicida pilD gene.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Boyd J.M., Knickle L., Touhami A., Dacanay A., Jericho M., Reith M.;
RT "Characterization of three type IV pili of Aeromonas salmonicida subsp.
RT salmonicida A449.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; U95640; AAC04561.1; -; Genomic_DNA.
DR EMBL; DQ396478; ABD57323.1; -; Genomic_DNA.
DR EMBL; CP000644; ABO88591.1; -; Genomic_DNA.
DR RefSeq; WP_005314162.1; NC_009348.1.
DR AlphaFoldDB; A2T195; -.
DR STRING; 382245.ASA_0411; -.
DR MEROPS; A24.001; -.
DR EnsemblBacteria; ABO88591; ABO88591; ASA_0411.
DR KEGG; asa:ASA_0411; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_0_0_6; -.
DR OMA; VFWLFKL; -.
DR OrthoDB; 2046608at2; -.
DR Proteomes; UP000000225; Chromosome.
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..291
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000289862"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT CONFLICT 60
FT /note="P -> A (in Ref. 1; AAC04561)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> G (in Ref. 1; AAC04561)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="C -> W (in Ref. 1; AAC04561)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="C -> W (in Ref. 1; AAC04561)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="A -> G (in Ref. 1; AAC04561)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="T -> N (in Ref. 1; AAC04561)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> R (in Ref. 1; AAC04561)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="L -> V (in Ref. 1; AAC04561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32501 MW; 4CFFA0AFC886E368 CRC64;
MTLLLELAHG LPWLYFSLVF LFSLMIGSFL NVVIHRLPIM LEREWQAEYR SYFSSDTPQP
EDDERYNLMV PRSCCPRCNH PITALENIPL LSWLWLKGRC RGCQAAISAR YPLVELLTAL
LSVVVAMTLT PGWGTLAALL LTWVLVALTF IDLDKMLLPD QLTLPLLWGG LLFNLLGGYV
PLGDAVIGAM AGYLVLWSLY WAFKLLTGKE GMGYGDFKLL AALGAWLGWQ ALPIVLLLSS
LVGAIFGIGL ILLRNHHQSK PIPFGPYLAI AGWIALLWGD SITRWYLSTI L
