UniProtKB - P02974 (FMM1_NEIGO)
Type IV major pilin protein PilE1
pilE1
Functioni
Major component of the type IV pilus (T4P) that plays a role in cellular adherence, microcolony formation, resistance to neutrophil mediated killing, twitching motility as well as transformation (PubMed:27213957).
Mediates the attachment and the formation of bacterial microcolonies on host epithelial cells. Mechanistically, pili retractation induces host NF-kappa-B activation in infected cells, which is temporally associated with the formation of gonococcal microcolonies (PubMed:27213957).
1 PublicationCaution
GO - Biological processi
- cell adhesion Source: UniProtKB-KW
Keywordsi
Biological process | Cell adhesion |
Names & Taxonomyi
Protein namesi | Recommended name: Type IV major pilin protein PilE1Alternative name(s): MS11 antigen Pilin |
Gene namesi | Name:pilE1 |
Organismi | Neisseria gonorrhoeae |
Taxonomic identifieri | 485 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Subcellular locationi
Other locations
- Fimbrium
- Membrane Sequence analysis; Single-pass membrane protein Sequence analysis
Other locations
- integral component of membrane Source: UniProtKB-KW
- pilus Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 8 – 28 | HelicalSequence analysisAdd BLAST | 21 |
Keywords - Cellular componenti
Fimbrium, MembranePathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 75 | S → A: Alters the morphology of fibers. 1 Publication | 1 | |
Mutagenesisi | 128 | C → G: Loss of pili. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04522, Dexfosfoserine DB04079, Heptane-1,2,3-Triol DB06838, methyl L-phenylalaninate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
PropeptideiPRO_0000024154 | 1 – 7 | Leader sequencePROSITE-ProRule annotation2 Publications | 7 | |
ChainiPRO_0000024155 | 8 – 165 | Type IV major pilin protein PilE1Add BLAST | 158 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 8 | N-methylphenylalaninePROSITE-ProRule annotation3 Publications | 1 | |
Glycosylationi | 70 | O-linked (DADDGlc) serine3 Publications | 1 | |
Modified residuei | 75 | O-(2-aminoethylphosphoryl)serine; alternate3 Publications | 1 | |
Modified residuei | 75 | O-(2-cholinephosphoryl)serine; alternate3 Publications | 1 | |
Modified residuei | 75 | Phosphoserine; alternate3 Publications | 1 | |
Modified residuei | 101 | O-(sn-1-glycerophosphoryl)serine; partial1 Publication | 1 | |
Disulfide bondi | 128 ↔ 158 | 1 Publication |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, Methylation, PhosphoproteinPTM databases
iPTMneti | P02974 |
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.
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P02974 |
SMRi | P02974 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P02974 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 137 – 165 | DisorderedSequence analysisAdd BLAST | 29 |
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
InterProi | View protein in InterPro IPR012902, N_methyl_site IPR001082, Pilin IPR045584, Pilin-like |
Pfami | View protein in Pfam PF07963, N_methyl, 1 hit PF00114, Pilin, 1 hit |
SUPFAMi | SSF54523, SSF54523, 1 hit |
TIGRFAMsi | TIGR02532, IV_pilin_GFxxxE, 1 hit |
PROSITEi | View protein in PROSITE PS00409, PROKAR_NTER_METHYL, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ
60 70 80 90 100
KSAVTEYYLN HGKWPENNTS AGVASPPSDI KGKYVKEVEV KNGVVTATML
110 120 130 140 150
SSGVNNEIKG KKLSLWARRE NGSVKWFCGQ PVTRTDDDTV ADAKDGKEID
160
TKHLPSTCRD NFDAK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 161 – 162 | NF → KAS (PubMed:6148752).Curated | 2 | |
Sequence conflicti | 161 – 162 | NF → KAS (PubMed:2872674).Curated | 2 | |
Sequence conflicti | 161 – 162 | NF → KAS (PubMed:1671354).Curated | 2 | |
Sequence conflicti | 161 – 162 | NF → KAS (PubMed:1348857).Curated | 2 | |
Sequence conflicti | 161 – 162 | NF → KAS (PubMed:6143785).Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K02078 Genomic DNA Translation: AAA25466.1 M13222 mRNA Translation: AAA25468.1 |
PIRi | A94007, YQNHG |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K02078 Genomic DNA Translation: AAA25466.1 M13222 mRNA Translation: AAA25468.1 |
PIRi | A94007, YQNHG |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AY2 | X-ray | 2.60 | A | 9-165 | [»] | |
2HI2 | X-ray | 2.30 | A | 8-165 | [»] | |
2HIL | electron microscopy | 12.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R | 8-165 | [»] | |
2PIL | X-ray | 2.60 | A | 8-165 | [»] | |
5VXX | electron microscopy | 5.10 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U | 8-165 | [»] | |
AlphaFoldDBi | P02974 | |||||
SMRi | P02974 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB04522, Dexfosfoserine DB04079, Heptane-1,2,3-Triol DB06838, methyl L-phenylalaninate |
PTM databases
iPTMneti | P02974 |
Miscellaneous databases
EvolutionaryTracei | P02974 |
Family and domain databases
InterProi | View protein in InterPro IPR012902, N_methyl_site IPR001082, Pilin IPR045584, Pilin-like |
Pfami | View protein in Pfam PF07963, N_methyl, 1 hit PF00114, Pilin, 1 hit |
SUPFAMi | SSF54523, SSF54523, 1 hit |
TIGRFAMsi | TIGR02532, IV_pilin_GFxxxE, 1 hit |
PROSITEi | View protein in PROSITE PS00409, PROKAR_NTER_METHYL, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | FMM1_NEIGO | |
Accessioni | P02974Primary (citable) accession number: P02974 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | November 1, 1995 | |
Last modified: | May 25, 2022 | |
This is version 126 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families