LEP4_BURP2
ID LEP4_BURP2 Reviewed; 309 AA.
AC I1WFC0; Q63QL3; Q9ZF70;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 32.
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=gspO; OrderedLocusNames=BP1026B_I0298;
OS Burkholderia pseudomallei (strain 1026b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=884204;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1026b;
RX PubMed=10419967; DOI=10.1128/jb.181.15.4661-4664.1999;
RA DeShazer D., Brett P.J., Burtnick M.N., Woods D.E.;
RT "Molecular characterization of genetic loci required for secretion of
RT exoproducts in Burkholderia pseudomallei.";
RL J. Bacteriol. 181:4661-4664(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1026b;
RX PubMed=22615773; DOI=10.1371/journal.pone.0036507;
RA Hayden H.S., Lim R., Brittnacher M.J., Sims E.H., Ramage E.R., Fong C.,
RA Wu Z., Crist E., Chang J., Zhou Y., Radey M., Rohmer L., Haugen E.,
RA Gillett W., Wuthiekanun V., Peacock S.J., Kaul R., Miller S.I., Manoil C.,
RA Jacobs M.A.;
RT "Evolution of Burkholderia pseudomallei in recurrent melioidosis.";
RL PLoS ONE 7:E36507-E36507(2012).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05189.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF110186; AAD05189.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002833; AFI64964.1; -; Genomic_DNA.
DR AlphaFoldDB; I1WFC0; -.
DR MEROPS; A24.A10; -.
DR EnsemblBacteria; AFI64964; AFI64964; BP1026B_I0298.
DR KEGG; bpz:BP1026B_I0298; -.
DR PATRIC; fig|884204.3.peg.307; -.
DR Proteomes; UP000010087; Chromosome 1.
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..309
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000429792"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
SQ SEQUENCE 309 AA; 32224 MW; 0429ACF8E7CA0783 CRC64;
MPTASMTPNP FLSGSPEHAA AAGPLAAFAA LPTGMQLAFA IVLGLVVGSF LNVVVHRLPI
MMKRAWLAEI AEATGAPCAD DSLPARYNLC VPRSACPHCG HALRAWENVP VLSYIALRGR
CRHCRTPIGA RYPLIELASG ALAAGALALF GPSGAALAAF GLCAALLAMS AIDMQTGFLP
DSLTLPLLWA GLCVNLWGTF ASLRAAVIGA IAGYLFLWCI LWLFKLLRGI EGIGYGDLKL
LAALGAWLGW EALPQVVLIA AVAGAAVGLV ATWRGRMRFE EPLPFGPFLA AGGAATLFFG
TPFYLLLGG
