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

pilE1

Organism
Neisseria gonorrhoeae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein is the predominant Neisseria surface antigen, which allows adhesion of the bacterium to various host cells.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Fimbrial protein
Alternative name(s):
MS11 antigen
Pilin
Gene namesi
Name:pilE1
OrganismiNeisseria gonorrhoeae
Taxonomic identifieri485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Fimbrium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi75 – 751S → A: Alters the morphology of fibers. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 772 PublicationsPRO_0000024154
Chaini8 – 165158Fimbrial proteinPRO_0000024155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81N-methylphenylalanine3 Publications
Glycosylationi70 – 701O-linked (DADDGlc...)2 Publications
Modified residuei75 – 751O-(2-aminoethylphosphoryl)serine; alternate3 Publications
Modified residuei75 – 751O-(2-cholinephosphoryl)serine; alternate3 Publications
Modified residuei75 – 751Phosphoserine; alternate3 Publications
Modified residuei101 – 1011O-(sn-1-glycerophosphoryl)serine; partial1 Publication
Disulfide bondi128 ↔ 1581 Publication

Post-translational modificationi

The O-linked glycan identified as Gal-GlcNAc disaccharide in PubMed:7477282 and PubMed:10048019 is now identified as either a hexosyl-diacetamidotrideoxyhexoside (DATDHex) by mass spectrometry in PubMed:15249686, or alpha-D-galactopyranosyl-(1->3)-2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranoside (DADDGlc) by X-ray diffraction in PubMed:16949362. It is not clear whether there is a chemical difference in the glycosylation of the two derivatives of strain MS11 used in these experiments, or not.2 Publications
In some MS11 derivative strains, Ser-75 is modified to O-(2-aminoethylphosphoryl)serine, and in some other derivatives that can be secondarily modified to O-(2-cholinephosphoryl)serine by N-methylation.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

PTM databases

iPTMnetiP02974.

Miscellaneous databases

PMAP-CutDBP02974.

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

STRINGi528354.NGFG_01821.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2718Combined sources
Turni28 – 303Combined sources
Helixi31 – 4717Combined sources
Helixi51 – 6111Combined sources
Helixi68 – 714Combined sources
Helixi77 – 793Combined sources
Beta strandi83 – 919Combined sources
Beta strandi94 – 996Combined sources
Beta strandi101 – 1044Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi112 – 1198Combined sources
Beta strandi121 – 13010Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi139 – 1424Combined sources
Helixi151 – 1533Combined sources
Beta strandi156 – 1583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AY2X-ray2.60A9-165[»]
2HI2X-ray2.30A8-165[»]
2HILelectron microscopy12.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R8-165[»]
2PILX-ray2.60A8-165[»]
ProteinModelPortaliP02974.
SMRiP02974. Positions 8-165.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02974.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108ZUW. Bacteria.
COG4969. LUCA.

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.

P02974-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:165
Mass (Da):17,944
Last modified:November 1, 1995 - v2
Checksum:iBCD3723C11AF5B4C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1622NF → KAS (PubMed:6148752).Curated
Sequence conflicti161 – 1622NF → KAS (PubMed:2872674).Curated
Sequence conflicti161 – 1622NF → KAS (PubMed:1671354).Curated
Sequence conflicti161 – 1622NF → KAS (PubMed:1348857).Curated
Sequence conflicti161 – 1622NF → KAS (PubMed:6143785).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02078 Genomic DNA. Translation: AAA25466.1.
M13222 mRNA. Translation: AAA25468.1.
PIRiA94007. YQNHG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02078 Genomic DNA. Translation: AAA25466.1.
M13222 mRNA. Translation: AAA25468.1.
PIRiA94007. YQNHG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AY2X-ray2.60A9-165[»]
2HI2X-ray2.30A8-165[»]
2HILelectron microscopy12.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R8-165[»]
2PILX-ray2.60A8-165[»]
ProteinModelPortaliP02974.
SMRiP02974. Positions 8-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi528354.NGFG_01821.

PTM databases

iPTMnetiP02974.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108ZUW. Bacteria.
COG4969. LUCA.

Miscellaneous databases

EvolutionaryTraceiP02974.
PMAP-CutDBP02974.

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...

Publicationsi

  1. "Pilus genes of Neisseria gonorrheae: chromosomal organization and DNA sequence."
    Meyer T.F., Billyard E., Haas R., Storzbach S., So M.
    Proc. Natl. Acad. Sci. U.S.A. 81:6110-6114(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MS11.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Phase variation of gonococcal pili by frameshift mutation in pilC, a novel gene for pilus assembly."
    Jonsson A.B., Nyberg G., Normark S.
    EMBO J. 10:477-488(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Neisseria gonorrhoeae PilC expression provides a selective mechanism for structural diversity of pili."
    Jonsson A.B., Pfeifer J., Normark S.
    Proc. Natl. Acad. Sci. U.S.A. 89:3204-3208(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid."
    Hermodson M.A., Chen K.C., Buchanan T.M.
    Biochemistry 17:442-445(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 8-36, METHYLATION AT PHE-8.
    Strain: 33, 7122, ATCC 33084 / F62 / M-1914 and B.
  6. "Gonococcal pili. Primary structure and receptor binding domain."
    Schoolnik G.K., Fernandez R., Tai J.Y., Rothbard J., Gotschlich E.C.
    J. Exp. Med. 159:1351-1370(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 8-165, PRESENCE OF PHOSPHORYLATION.
    Strain: MS11.
  7. "Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili."
    Hegge F.T., Hitchen P.G., Aas F.E., Kristiansen H., Lovold C., Egge-Jacobsen W., Panico M., Leong W.Y., Bull V., Virji M., Morris H.R., Dell A., Koomey M.
    Proc. Natl. Acad. Sci. U.S.A. 101:10798-10803(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-75.
    Strain: MS11.
  8. "Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical modifications with phosphoethanolamine and phosphocholine requiring an enzyme structurally related to lipopolysaccharide phosphoethanolamine transferases."
    Aas F.E., Egge-Jacobsen W., Winther-Larsen H.C., Lovold C., Hitchen P.G., Dell A., Koomey M.
    J. Biol. Chem. 281:27712-27723(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-75.
    Strain: MS11.
  9. "Structure of the fibre-forming protein pilin at 2.6-A resolution."
    Parge H.E., Forest K.T., Hickey M.J., Christensen D.A., Getzoff E., Tainer J.A.
    Nature 378:32-38(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 8-165, METHYLATION AT PHE-8, GLYCOSYLATION AT SER-70, SEQUENCE REVISION TO C-TERMINUS.
    Strain: MS11.
  10. "Crystallographic structure reveals phosphorylated pilin from Neisseria: phosphoserine sites modify type IV pilus surface chemistry and fibre morphology."
    Forest K.T., Dunham S.A., Koomey M., Tainer J.A.
    Mol. Microbiol. 31:743-752(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 8-165, PHOSPHORYLATION AT SER-75, GLYCOSYLATION AT SER-70, PHOSPHORYLATION AT SER-101, MUTAGENESIS OF SER-75, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: MS11.
  11. "Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions."
    Craig L., Volkmann N., Arvai A.S., Pique M.E., Yeager M., Egelman E.H., Tainer J.A.
    Mol. Cell 23:651-662(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON CRYOMICROSCOPY (12.5 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 8-165.
    Strain: MS11.

Entry informationi

Entry nameiFMM1_NEIGO
AccessioniPrimary (citable) accession number: P02974
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

In PubMed:413571 it is said that 50% of the peptides have N-methyl-Phe and 50% begin with Thr-9. N-terminal methylation produces preview during Edman degradation, which makes this appear to happen when the peptide is completely N-terminal methylated.Curated

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.