PAPE_ECOLX
ID PAPE_ECOLX Reviewed; 173 AA.
AC P08407;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Fimbrial protein PapE;
DE Flags: Precursor;
GN Name=papE;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700336 / J96 / UPEC;
RX PubMed=2869489; DOI=10.1073/pnas.83.6.1891;
RA Lindberg F., Lund B., Normark S.;
RT "Gene products specifying adhesion of uropathogenic Escherichia coli are
RT minor components of pili.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1891-1895(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700336 / J96 / UPEC;
RX PubMed=2895103; DOI=10.1128/jb.170.4.1887-1894.1988;
RA Lund B., Lindberg F., Normark S.;
RT "Structure and antigenic properties of the tip-located P pilus proteins of
RT uropathogenic Escherichia coli.";
RL J. Bacteriol. 170:1887-1894(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700336 / J96 / UPEC;
RX PubMed=1357526; DOI=10.1111/j.1365-2958.1992.tb01399.x;
RA Marklund B.-I., Tennent J.M., Garcia E., Hamers A., Baga M., Lindberg F.,
RA Gaastra W., Normark S.;
RT "Horizontal gene transfer of the Escherichia coli pap and prs pili operons
RT as a mechanism for the development of tissue-specific adhesive
RT properties.";
RL Mol. Microbiol. 6:2225-2242(1992).
RN [4]
RP SUBUNIT.
RX PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
RA Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
RT "The chaperone-assisted membrane release and folding pathway is sensed by
RT two signal transduction systems.";
RL EMBO J. 16:6394-6406(1997).
RN [5]
RP DEGRADATION BY DEGP, SUBUNIT, AND MUTAGENESIS OF 2-LYS--MET-12.
RX PubMed=16303867; DOI=10.1073/pnas.0508936102;
RA Isaac D.D., Pinkner J.S., Hultgren S.J., Silhavy T.J.;
RT "The extracytoplasmic adaptor protein CpxP is degraded with substrate by
RT DegP.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17775-17779(2005).
RN [6]
RP INTERACTION WITH CPXP.
RX PubMed=25207645; DOI=10.1371/journal.pone.0107383;
RA Tschauner K., Hoernschemeyer P., Mueller V.S., Hunke S.;
RT "Dynamic interaction between the CpxA sensor kinase and the periplasmic
RT accessory protein CpxP mediates signal recognition in E. coli.";
RL PLoS ONE 9:E107383-E107383(2014).
RN [7]
RP REVIEW.
RX PubMed=10049807; DOI=10.1006/jsbi.1998.4049;
RA Hung D.L., Hultgren S.J.;
RT "Pilus biogenesis via the chaperone/usher pathway: an integration of
RT structure and function.";
RL J. Struct. Biol. 124:201-220(1998).
CC -!- FUNCTION: Repeated PapE subunits make up the thin (2 nm in diameter)
CC tip fibrillum of the P pilus. Subunits are arranged in a open helical
CC conformation. Pili with a defective papE gene have low adhesive
CC capacity or none; however, the binding property of the whole cell is
CC not affected. Pili are polar filaments radiating from the surface of
CC the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300
CC per cell, and enable bacteria to colonize the epithelium of specific
CC host organs.
CC -!- SUBUNIT: Probably interacts with chaperone PapD. Assembly of the P
CC pilus requires periplasmic chaperone PapD, in absence of the chaperone
CC overexpression of this subunit is toxic, with PapE accumulating in the
CC periplasm (PubMed:9351822). Misfolded protein interacts with CpxP,
CC which probably targets it for degradation (PubMed:25207645).
CC {ECO:0000269|PubMed:25207645, ECO:0000269|PubMed:9351822}.
CC -!- INTERACTION:
CC P08407; P15319: papD; NbExp=2; IntAct=EBI-1034986, EBI-1034993;
CC -!- SUBCELLULAR LOCATION: Secreted. Fimbrium. Note=At the tip of the P
CC pilus.
CC -!- PTM: Overexpression of this protein in the absence of chaperone PapD
CC leads to proteolysis of itself and CpxP; degradation requires both cpxP
CC and degP, as well as the N-terminus of PapE (PubMed:16303867).
CC {ECO:0000269|PubMed:16303867}.
CC -!- MISCELLANEOUS: Strains of E.coli that cause infection of the human
CC urinary tract produce pap-pili (P pili) which are hair-like appendages
CC consisting of about 1000 helically arranged subunits of the protein
CC PapA. These pili mediate binding to digalactoside-containing
CC glycolipids present on the epithelial cells which line the urinary
CC tract.
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; X61238; CAA43556.1; -; Genomic_DNA.
DR EMBL; M13239; AAA24280.1; -; Genomic_DNA.
DR EMBL; M20146; AAA24288.1; -; Genomic_DNA.
DR EMBL; X61239; CAA43568.1; -; Genomic_DNA.
DR PIR; A25134; YQECPE.
DR RefSeq; WP_000723802.1; NZ_WVVH01000110.1.
DR PDB; 1N0L; X-ray; 2.30 A; B/D=37-173.
DR PDB; 1N12; X-ray; 1.87 A; A/C=37-173.
DR PDBsum; 1N0L; -.
DR PDBsum; 1N12; -.
DR AlphaFoldDB; P08407; -.
DR SMR; P08407; -.
DR DIP; DIP-37855N; -.
DR IntAct; P08407; 3.
DR OMA; HAKLGYK; -.
DR EvolutionaryTrace; P08407; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1090; -; 1.
DR InterPro; IPR000259; Adhesion_dom_fimbrial.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR004086; P_pili_tip_fibrillum_PapE.
DR Pfam; PF00419; Fimbrial; 1.
DR PRINTS; PR01555; FIMBRIALPAPE.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Fimbrium; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..173
FT /note="Fimbrial protein PapE"
FT /id="PRO_0000022003"
FT MUTAGEN 2..12
FT /note="Missing: No longer leads to CpxP degradation, i.e.
FT periplasmic proteolysis is altered."
FT /evidence="ECO:0000269|PubMed:16303867"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:1N12"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1N0L"
FT STRAND 136..152
FT /evidence="ECO:0007829|PDB:1N12"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1N12"
FT STRAND 160..172
FT /evidence="ECO:0007829|PDB:1N12"
SQ SEQUENCE 173 AA; 18569 MW; E27577D09C46A863 CRC64;
MKKIRGLCLP VMLGAVLMSQ HVHAVDNLTF RGKLIIPACT VSNTTVDWQD VEIQTLSQNG
NHEKEFTVNM RCPYNLGTMK VTITATNTYN NAILVQNTSN TSSDGLLVYL YNSNAGNIGT
AITLGTPFTP GKITGNNADK TISLHAKLGY KGNMQNLIAG PFSATATLVA SYS
