Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fimbrial protein

Gene

pilA

Organism
Pseudomonas aeruginosa
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Fimbrial protein
Alternative name(s):
Pilin
Gene namesi
Name:pilA
Synonyms:fimA
OrganismiPseudomonas aeruginosa
Taxonomic identifieri287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

  • pilus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Fimbrium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 661 PublicationPRO_0000024176
Chaini7 – 150144Fimbrial proteinPRO_0000024177Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71N-methylphenylalanine1 Publication
Disulfide bondi135 ↔ 148

Keywords - PTMi

Disulfide bond, Methylation

Interactioni

Subunit structurei

The pili are polar flexible filaments of about 5.4 nanometers diameter and 2.5 micrometers average length; they consist of only a single polypeptide chain arranged in a helical configuration of five subunits per turn in the assembled pilus.

Protein-protein interaction databases

IntActiP02973. 1 interaction.

Structurei

Secondary structure

1
150
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 4612Combined sources
Helixi49 – 5810Combined sources
Beta strandi62 – 687Combined sources
Turni72 – 754Combined sources
Beta strandi76 – 783Combined sources
Beta strandi90 – 989Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi104 – 1096Combined sources
Turni115 – 1195Combined sources
Beta strandi121 – 1266Combined sources
Turni128 – 1303Combined sources
Beta strandi133 – 1375Combined sources
Helixi141 – 1433Combined sources
Turni146 – 1483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZOX-ray1.63A35-150[»]
1NILNMR-A134-149[»]
1NIMNMR-A134-149[»]
1OQWX-ray2.00A/B7-150[»]
1PAJNMR-A134-149[»]
1PAKNMR-A134-149[»]
1X6PX-ray1.63A35-150[»]
1X6QX-ray1.51A35-150[»]
1X6RX-ray1.82A35-150[»]
1X6XX-ray0.96X35-150[»]
1X6YX-ray1.55A35-150[»]
1X6ZX-ray0.78A35-150[»]
2PY0X-ray1.35A35-149[»]
ProteinModelPortaliP02973.
SMRiP02973. Positions 7-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02973.

Family & Domainsi

Sequence similaritiesi

Belongs to the N-Me-Phe pilin family.Curated

Family and domain databases

InterProiIPR012902. N_methyl_site.
IPR001082. Pilin.
[Graphical view]
PfamiPF13633. N_methyl_3. 1 hit.
PF00114. Pilin. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02532. IV_pilin_GFxxxE. 1 hit.
PROSITEiPS00409. PROKAR_NTER_METHYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02973-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAQKGFTLI ELMIVVAIIG ILAAIAIPQY QNYVARSEGA SALASVNPLK
60 70 80 90 100
TTVEEALSRG WSVKSGTGTE DATKKEVPLG VAADANKLGT IALKPDPADG
110 120 130 140 150
TADITLTFTM GGAGPKNKGK IITLTRTAAD GLWKCTSDQD EQFIPKGCSR
Length:150
Mass (Da):15,650
Last modified:November 1, 1990 - v2
Checksum:iC0E35B69FD6FBE84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901T → TS AA sequence (PubMed:6131838).Curated
Sequence conflicti101 – 1033TAD → DTA AA sequence (PubMed:6131838).Curated
Sequence conflicti128 – 1281A → D in AAM26730 (PubMed:7903973).Curated
Sequence conflicti150 – 1501R → K in AAA25955 (PubMed:2430961).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14849 Genomic DNA. Translation: AAA25955.1.
X02402 Genomic DNA. Translation: CAA26248.1.
S67807 Genomic DNA. Translation: AAM26730.1.
PIRiA24603. YQPSPA.
RefSeqiWP_058135760.1. NZ_LLUB01000003.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14849 Genomic DNA. Translation: AAA25955.1.
X02402 Genomic DNA. Translation: CAA26248.1.
S67807 Genomic DNA. Translation: AAM26730.1.
PIRiA24603. YQPSPA.
RefSeqiWP_058135760.1. NZ_LLUB01000003.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZOX-ray1.63A35-150[»]
1NILNMR-A134-149[»]
1NIMNMR-A134-149[»]
1OQWX-ray2.00A/B7-150[»]
1PAJNMR-A134-149[»]
1PAKNMR-A134-149[»]
1X6PX-ray1.63A35-150[»]
1X6QX-ray1.51A35-150[»]
1X6RX-ray1.82A35-150[»]
1X6XX-ray0.96X35-150[»]
1X6YX-ray1.55A35-150[»]
1X6ZX-ray0.78A35-150[»]
2PY0X-ray1.35A35-149[»]
ProteinModelPortaliP02973.
SMRiP02973. Positions 7-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02973. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02973.

Family and domain databases

InterProiIPR012902. N_methyl_site.
IPR001082. Pilin.
[Graphical view]
PfamiPF13633. N_methyl_3. 1 hit.
PF00114. Pilin. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02532. IV_pilin_GFxxxE. 1 hit.
PROSITEiPS00409. PROKAR_NTER_METHYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFMPA_PSEAI
AccessioniPrimary (citable) accession number: P02973
Secondary accession number(s): Q53390
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: May 11, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.