LEP4_VIBCH
ID LEP4_VIBCH Reviewed; 253 AA.
AC P0C6D9; P27717; Q56668; Q9JQ05;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=VC_0839;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC STRAIN=Classical Inaba Z17561 / Serotype O1;
RX PubMed=1352761; DOI=10.1016/0378-1119(92)90634-2;
RA Ogierman M.A., Manning P.A.;
RT "Homology of TcpN, a putative regulatory protein of Vibrio cholerae, to the
RT AraC family of transcriptional activators.";
RL Gene 116:93-97(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RC STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RX PubMed=1400247; DOI=10.1128/jb.174.21.6974-6980.1992;
RA Higgins D.E., Nazareno E., DiRita V.J.;
RT "The virulence gene activator ToxT from Vibrio cholerae is a member of the
RT AraC family of transcriptional activators.";
RL J. Bacteriol. 174:6974-6980(1992).
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; AE003852; AAF94002.1; -; Genomic_DNA.
DR EMBL; X64098; CAA45466.1; -; Genomic_DNA.
DR EMBL; L01623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A40582; A40582.
DR PIR; D82273; D82273.
DR RefSeq; NP_230487.1; NC_002505.1.
DR RefSeq; WP_000456980.1; NZ_LT906614.1.
DR AlphaFoldDB; P0C6D9; -.
DR STRING; 243277.VC_0839; -.
DR MEROPS; A24.001; -.
DR DNASU; 2614506; -.
DR EnsemblBacteria; AAF94002; AAF94002; VC_0839.
DR GeneID; 57739541; -.
DR KEGG; vch:VC_0839; -.
DR PATRIC; fig|243277.26.peg.800; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_0_1_6; -.
DR OMA; RGKCAFC; -.
DR BioCyc; VCHO:VC0839-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
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:0006465; P:signal peptide processing; IBA:GO_Central.
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; Reference proteome;
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_0000192629"
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 72
FT /note="K -> N (in Ref. 2; CAA45466)"
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
