PPPA_ECOH1
ID PPPA_ECOH1 Reviewed; 269 AA.
AC E3PJ89;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Type 4 prepilin-like proteins leader peptide-processing enzyme {ECO:0000255|RuleBase:RU003794};
DE EC=2.1.1.- {ECO:0000255|RuleBase:RU003794};
DE EC=3.4.23.43 {ECO:0000255|RuleBase:RU003794};
GN Name=pppA {ECO:0000303|PubMed:22585966}; OrderedLocusNames=ETEC_3240;
OS Escherichia coli O78:H11 (strain H10407 / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316401;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H10407 / ETEC;
RX PubMed=20802035; DOI=10.1128/jb.00710-10;
RA Crossman L.C., Chaudhuri R.R., Beatson S.A., Wells T.J., Desvaux M.,
RA Cunningham A.F., Petty N.K., Mahon V., Brinkley C., Hobman J.L.,
RA Savarino S.J., Turner S.M., Pallen M.J., Penn C.W., Parkhill J.,
RA Turner A.K., Johnson T.J., Thomson N.R., Smith S.G., Henderson I.R.;
RT "A commensal gone bad: complete genome sequence of the prototypical
RT enterotoxigenic Escherichia coli strain H10407.";
RL J. Bacteriol. 192:5822-5831(2010).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=H10407 / ETEC;
RX PubMed=22585966; DOI=10.1128/iai.06394-11;
RA Strozen T.G., Li G., Howard S.P.;
RT "YghG (GspSbeta) is a novel pilot protein required for localization of the
RT GspSbeta type II secretion system secretin of enterotoxigenic Escherichia
RT coli.";
RL Infect. Immun. 80:2608-2622(2012).
CC -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates the N-
CC terminal (generally Phe) residue. {ECO:0000255|RuleBase:RU003794}.
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:0000255|RuleBase:RU003794};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No effect on assembly of T2SS-beta, severely
CC reduced secretion of the labile toxin exported by T2SS-beta.
CC {ECO:0000269|PubMed:22585966}.
CC -!- MISCELLANEOUS: Encoded in a type II secretion system (T2SS-beta); this
CC strain encodes 2 T2SS but only this one (beta) is expressed under
CC standard laboratory conditions. {ECO:0000305|PubMed:22585966}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family.
CC {ECO:0000255|RuleBase:RU003793}.
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DR EMBL; FN649414; CBJ02740.1; -; Genomic_DNA.
DR RefSeq; WP_014640016.1; NC_017633.1.
DR AlphaFoldDB; E3PJ89; -.
DR MEROPS; A24.A01; -.
DR EnsemblBacteria; CBJ02740; CBJ02740; ETEC_3240.
DR KEGG; elh:ETEC_3240; -.
DR HOGENOM; CLU_057101_0_0_6; -.
DR OMA; VFWLFKL; -.
DR Proteomes; UP000006877; 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: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; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..269
FT /note="Type 4 prepilin-like proteins leader peptide-
FT processing enzyme"
FT /id="PRO_0000446501"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 269 AA; 29494 MW; 86469596500901F0 CRC64;
MLFDVFQQYP AAMPVLATVG GLIIGSFLNV VIWRYPIMLR QQMAEFHGEM PSVQSKISLA
LPRSHCPHCQ QTIRIRDNIP LLSWLMLKGR CRDCQAKISK RYPLVELLTA LAFLLASLVW
PESGWALAVM ILSAWLIAAS VIDLDHQWLP DVFTQGVLWT GLIAAWAQQS PLTLQDAVTG
VLVGFIAFYS LRWIAGIVLR KEALGMGDVL LFAALGSWVG PLSLPNVALI ASCCGLIYAV
ITKRGTTTLP FGPCLSLGGI ATIYLQALF
