LEP4_VIBC3
ID LEP4_VIBC3 Reviewed; 253 AA.
AC A5F385; C3LYK4; P27717; Q56668; Q9JQ05;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=tcpJ; OrderedLocusNames=VC0395_A0364, VC395_0855;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1680773; DOI=10.1101/gad.5.10.1834;
RA Kaufman M.R., Seyer J.M., Taylor R.K.;
RT "Processing of TCP pilin by TcpJ typifies a common step intrinsic to a
RT newly recognized pathway of extracellular protein secretion by Gram-
RT negative bacteria.";
RL Genes Dev. 5:1834-1846(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7894059; DOI=10.3109/10425179409039704;
RA Everiss K.D., Hughes K.J., Peterson K.M.;
RT "The accessory colonization factor and toxin-coregulated pilus gene
RT clusters are physically linked on the Vibrio cholerae O395 chromosome.";
RL DNA Seq. 5:51-55(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11179381; DOI=10.1128/iai.69.3.1947-1952.2001;
RA Karaolis D.K.R., Lan R., Kaper J.B., Reeves P.R.;
RT "Comparison of Vibrio cholerae pathogenicity islands in sixth and seventh
RT pandemic strains.";
RL Infect. Immun. 69:1947-1952(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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; M74708; AAA63557.1; -; Genomic_DNA.
DR EMBL; L25661; AAA69695.1; -; Genomic_DNA.
DR EMBL; AF325733; AAK20766.1; -; Genomic_DNA.
DR EMBL; CP000627; ABQ19617.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP08870.1; -; Genomic_DNA.
DR PIR; A40582; A40582.
DR RefSeq; WP_000456980.1; NZ_JAACZH010000023.1.
DR AlphaFoldDB; A5F385; -.
DR STRING; 345073.VC395_0855; -.
DR MEROPS; A24.001; -.
DR MEROPS; A24.019; -.
DR EnsemblBacteria; ABQ19617; ABQ19617; VC0395_A0364.
DR GeneID; 57739541; -.
DR KEGG; vco:VC0395_A0364; -.
DR KEGG; vcr:VC395_0855; -.
DR PATRIC; fig|345073.21.peg.827; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_0_1_6; -.
DR OMA; RGKCAFC; -.
DR Proteomes; UP000000249; Chromosome 2.
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..253
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000321862"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT CONFLICT 149..151
FT /note="QNP -> PNQ (in Ref. 1; AAA63557)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="S -> T (in Ref. 1; AAA63557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 29337 MW; 02C90A7F20061A70 CRC64;
MEYVYLILFS IVSLILGSFS NVVIYRLPRK ILLKNHFFYD IDSNRSMCPK CGNKISWYDN
VPLLSYLLLH GKCRHCDEKI SLSYFIVELS FFIIAFPIYW LSTDWVDSFV LLGLYFILFN
LFVIDFKSML LPNLLTYPIF MLAFIYVQQN PALTVESSII GGFAAFIISY VSNFIVRLFK
RIDVMGGGDI KLYTAIGTLI GVEFVPYLFL LSSIIAFIHW FFARVSCRYC LYIPLGPSII
ISFVIVFFSI RLM
