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Protein

Pap fimbrial major pilin protein

Gene

papA

Organism
Escherichia coli
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Polymerizes to form the thick (6.8 nm in diameter) rod of the pilus (also called fimbria). The rod is a right-handed helical cylinder with 3.28 PapA subunits per turn. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs.

Miscellaneous

Strains of E.coli that cause infection of the human urinary tract produce pap-pili which are hair-like appendages consisting of about 1000 helically arranged subunits of the protein PapA. These pili mediate binding to digalactoside-containing glycolipids present on the epithelial cells which line the urinary tract.

GO - Biological processi

Names & Taxonomyi

Protein namesi
Recommended name:
Pap fimbrial major pilin protein
Short name:
Pap pili
Gene namesi
Name:papA
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Fimbrium, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Add BLAST22
ChainiPRO_000000919723 – 185Pap fimbrial major pilin proteinAdd BLAST163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi44 ↔ 831 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

DIPiDIP-44594N
IntActiP04127, 4 interactors
MINTiP04127

Structurei

Secondary structure

1185
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 40Combined sources8
Beta strandi45 – 47Combined sources3
Beta strandi54 – 56Combined sources3
Helixi62 – 67Combined sources6
Beta strandi74 – 83Combined sources10
Beta strandi98 – 104Combined sources7
Beta strandi111 – 116Combined sources6
Beta strandi118 – 121Combined sources4
Beta strandi123 – 128Combined sources6
Beta strandi130 – 133Combined sources4
Beta strandi137 – 140Combined sources4
Beta strandi152 – 161Combined sources10
Beta strandi175 – 184Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UY6X-ray2.50B/C23-185[»]
2UY7X-ray2.60B/D/F/H23-185[»]
5FLUelectron microscopy3.80A/B/C/D/E/F/G/H/I/J/K/L/M23-185[»]
ProteinModelPortaliP04127
SMRiP04127
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04127

Family & Domainsi

Sequence similaritiesi

Belongs to the fimbrial protein family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1090, 1 hit
InterProiView protein in InterPro
IPR000259 Adhesion_dom_fimbrial
IPR036937 Adhesion_dom_fimbrial_sf
IPR008966 Adhesion_dom_sf
PfamiView protein in Pfam
PF00419 Fimbrial, 1 hit
SUPFAMiSSF49401 SSF49401, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04127-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKSVIAGAV AMAVVSFGVN NAAPTIPQGQ GKVTFNGTVV DAPCSISQKS
60 70 80 90 100
ADQSIDFGQL SKSFLEAGGV SKPMDLDIEL VNCDITAFKG GNGAKKGTVK
110 120 130 140 150
LAFTGPIVNG HSDELDTNGG TGTAIVVQGA GKNVVFDGSE GDANTLKDGE
160 170 180
NVLHYTAVVK KSSAVGAAVT EGAFSAVANF NLTYQ
Length:185
Mass (Da):18,686
Last modified:November 1, 1986 - v1
Checksum:i93DB4FFDA211C671
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03391 Genomic DNA Translation: CAA27126.1
X61239 Genomic DNA Translation: CAA43562.1
PIRiA23221 YQECPP

Similar proteinsi

Entry informationi

Entry nameiPAPA_ECOLX
AccessioniPrimary (citable) accession number: P04127
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: May 23, 2018
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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