PPPA_ECOLI
ID PPPA_ECOLI Reviewed; 269 AA.
AC Q46836; Q2M9M3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Prepilin peptidase PppA;
GN Name=pppA; Synonyms=yghH; OrderedLocusNames=b2972, JW2939;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: A pre-pilin peptidase involved in a type II secretion system
CC (T2SS, formerly general secretion pathway, GSP) for the export of
CC folded proteins across the outer membrane. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: In many other E.coli strains this gene is part of a type
CC II secretion system, but in MG1655 the locus is missing a number of
CC genes. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69139.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U28377; AAA69139.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76008.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77033.1; -; Genomic_DNA.
DR PIR; B65083; B65083.
DR RefSeq; NP_417446.4; NC_000913.3.
DR RefSeq; WP_001333829.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46836; -.
DR BioGRID; 4261823; 163.
DR STRING; 511145.b2972; -.
DR MEROPS; A24.A01; -.
DR TCDB; 1.A.54.5.4; the presenilin er ca(2+) leak channel (presenilin) family.
DR PaxDb; Q46836; -.
DR PRIDE; Q46836; -.
DR EnsemblBacteria; AAC76008; AAC76008; b2972.
DR EnsemblBacteria; BAE77033; BAE77033; BAE77033.
DR GeneID; 947467; -.
DR KEGG; ecj:JW2939; -.
DR KEGG; eco:b2972; -.
DR PATRIC; fig|1411691.4.peg.3759; -.
DR EchoBASE; EB2816; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_0_0_6; -.
DR InParanoid; Q46836; -.
DR OMA; VFWLFKL; -.
DR PhylomeDB; Q46836; -.
DR BioCyc; EcoCyc:G7539-MON; -.
DR PRO; PR:Q46836; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Prepilin peptidase PppA"
FT /id="PRO_0000192634"
FT TOPO_DOM 1..14
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..124
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..218
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..269
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 269 AA; 29466 MW; E793FD8B4C81F6A4 CRC64;
MLFDVFQQYP TAMPVLATVG GLIIGSFLNV VIWRYPIMLR QQMAEFHGEM SSAQSKISLA
LPRSHCPHCQ QTIRIRDNIP LFSWLMLKGR CRDCQAKISK RYPLVELLTA LAFLLASLVW
PESGWGLAVM ILSAWLIAAS VIDLDHQWLP DVFTQGVLWT GLIAAWAQQS PLTLQDAVTG
VLVGFITFYS LRWIAGIVLR KEALGMGDVL LFAALGGWVG ALSLPNVALI ASCCGLIYAV
ITKRGSTTLP FGPCLSLGGI ATLYLQALF
