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Fimbrial protein (MS11 antigen) (Pilin)

 FMM1_NEIGO              Reviewed;         165 AA.
P02974;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
05-JUL-2017, entry version 114.
RecName: Full=Fimbrial protein;
AltName: Full=MS11 antigen;
AltName: Full=Pilin;
Flags: Precursor;
Name=pilE1;
Neisseria gonorrhoeae.
Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
Neisseriaceae; Neisseria.
NCBI_TaxID=485;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MS11;
PubMed=6148752; DOI=10.1073/pnas.81.19.6110;
Meyer T.F., Billyard E., Haas R., Storzbach S., So M.;
"Pilus genes of Neisseria gonorrheae: chromosomal organization and DNA
sequence.";
Proc. Natl. Acad. Sci. U.S.A. 81:6110-6114(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2872674; DOI=10.1073/pnas.83.11.3890;
Bergstroem S., Robbins K., Koomey J.M., Swanson J.;
"Piliation control mechanisms in Neisseria gonorrhoeae.";
Proc. Natl. Acad. Sci. U.S.A. 83:3890-3894(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1671354;
Jonsson A.B., Nyberg G., Normark S.;
"Phase variation of gonococcal pili by frameshift mutation in pilC, a
novel gene for pilus assembly.";
EMBO J. 10:477-488(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1348857; DOI=10.1073/pnas.89.8.3204;
Jonsson A.B., Pfeifer J., Normark S.;
"Neisseria gonorrhoeae PilC expression provides a selective mechanism
for structural diversity of pili.";
Proc. Natl. Acad. Sci. U.S.A. 89:3204-3208(1992).
[5]
PROTEIN SEQUENCE OF 8-36, AND METHYLATION AT PHE-8.
STRAIN=33, 7122, ATCC 33084 / F62 / M-1914, and B;
PubMed=413571; DOI=10.1021/bi00596a010;
Hermodson M.A., Chen K.C., Buchanan T.M.;
"Neisseria pili proteins: amino-terminal amino acid sequences and
identification of an unusual amino acid.";
Biochemistry 17:442-445(1978).
[6]
PROTEIN SEQUENCE OF 8-165, AND PRESENCE OF PHOSPHORYLATION.
STRAIN=MS11;
PubMed=6143785; DOI=10.1084/jem.159.5.1351;
Schoolnik G.K., Fernandez R., Tai J.Y., Rothbard J., Gotschlich E.C.;
"Gonococcal pili. Primary structure and receptor binding domain.";
J. Exp. Med. 159:1351-1370(1984).
[7]
PHOSPHORYLATION AT SER-75.
STRAIN=MS11;
PubMed=15249686; DOI=10.1073/pnas.0402397101;
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.;
"Unique modifications with phosphocholine and phosphoethanolamine
define alternate antigenic forms of Neisseria gonorrhoeae type IV
pili.";
Proc. Natl. Acad. Sci. U.S.A. 101:10798-10803(2004).
[8]
PHOSPHORYLATION AT SER-75.
STRAIN=MS11;
PubMed=16825186; DOI=10.1074/jbc.M604324200;
Aas F.E., Egge-Jacobsen W., Winther-Larsen H.C., Lovold C.,
Hitchen P.G., Dell A., Koomey M.;
"Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical
modifications with phosphoethanolamine and phosphocholine requiring an
enzyme structurally related to lipopolysaccharide phosphoethanolamine
transferases.";
J. Biol. Chem. 281:27712-27723(2006).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 8-165, METHYLATION AT PHE-8,
GLYCOSYLATION AT SER-70, AND SEQUENCE REVISION TO C-TERMINUS.
STRAIN=MS11;
PubMed=7477282; DOI=10.1038/378032a0;
Parge H.E., Forest K.T., Hickey M.J., Christensen D.A., Getzoff E.,
Tainer J.A.;
"Structure of the fibre-forming protein pilin at 2.6-A resolution.";
Nature 378:32-38(1995).
[10]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=MS11;
PubMed=10048019; DOI=10.1046/j.1365-2958.1999.01184.x;
Forest K.T., Dunham S.A., Koomey M., Tainer J.A.;
"Crystallographic structure reveals phosphorylated pilin from
Neisseria: phosphoserine sites modify type IV pilus surface chemistry
and fibre morphology.";
Mol. Microbiol. 31:743-752(1999).
[11]
ELECTRON CRYOMICROSCOPY (12.5 ANGSTROMS), GLYCOSYLATION AT SER-70, AND
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 8-165.
STRAIN=MS11;
PubMed=16949362; DOI=10.1016/j.molcel.2006.07.004;
Craig L., Volkmann N., Arvai A.S., Pique M.E., Yeager M.,
Egelman E.H., Tainer J.A.;
"Type IV pilus structure by cryo-electron microscopy and
crystallography: implications for pilus assembly and functions.";
Mol. Cell 23:651-662(2006).
-!- FUNCTION: This protein is the predominant Neisseria surface
antigen, which allows adhesion of the bacterium to various host
cells.
-!- SUBUNIT: 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.
-!- SUBCELLULAR LOCATION: Fimbrium.
-!- PTM: 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.
{ECO:0000269|PubMed:10048019, ECO:0000269|PubMed:7477282}.
-!- PTM: 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. {ECO:0000269|PubMed:413571,
ECO:0000269|PubMed:7477282}.
-!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
-!- 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.
{ECO:0000305}.
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EMBL; K02078; AAA25466.1; -; Genomic_DNA.
EMBL; M13222; AAA25468.1; -; mRNA.
PIR; A94007; YQNHG.
PDB; 1AY2; X-ray; 2.60 A; A=9-165.
PDB; 2HI2; X-ray; 2.30 A; A=8-165.
PDB; 2HIL; EM; 12.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=8-165.
PDB; 2PIL; X-ray; 2.60 A; A=8-165.
PDBsum; 1AY2; -.
PDBsum; 2HI2; -.
PDBsum; 2HIL; -.
PDBsum; 2PIL; -.
ProteinModelPortal; P02974; -.
SMR; P02974; -.
DrugBank; DB06838; methyl L-phenylalaninate.
DrugBank; DB04522; Phosphonoserine.
iPTMnet; P02974; -.
eggNOG; ENOG4108ZUW; Bacteria.
eggNOG; COG4969; LUCA.
EvolutionaryTrace; P02974; -.
PMAP-CutDB; P02974; -.
GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
InterPro; IPR012902; N_methyl_site.
InterPro; IPR001082; Pilin.
Pfam; PF07963; N_methyl; 1.
Pfam; PF00114; Pilin; 1.
TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Direct protein sequencing;
Disulfide bond; Fimbrium; Glycoprotein; Methylation; Phosphoprotein.
PROPEP 1 7 {ECO:0000269|PubMed:413571,
ECO:0000269|PubMed:6143785}.
/FTId=PRO_0000024154.
CHAIN 8 165 Fimbrial protein.
/FTId=PRO_0000024155.
MOD_RES 8 8 N-methylphenylalanine.
{ECO:0000269|PubMed:413571,
ECO:0000269|PubMed:6143785,
ECO:0000269|PubMed:7477282}.
MOD_RES 75 75 O-(2-aminoethylphosphoryl)serine;
alternate. {ECO:0000269|PubMed:10048019,
ECO:0000269|PubMed:15249686,
ECO:0000269|PubMed:16825186}.
MOD_RES 75 75 O-(2-cholinephosphoryl)serine; alternate.
{ECO:0000269|PubMed:10048019,
ECO:0000269|PubMed:15249686,
ECO:0000269|PubMed:16825186}.
MOD_RES 75 75 Phosphoserine; alternate.
{ECO:0000269|PubMed:10048019,
ECO:0000269|PubMed:15249686,
ECO:0000269|PubMed:16825186}.
MOD_RES 101 101 O-(sn-1-glycerophosphoryl)serine;
partial. {ECO:0000269|PubMed:10048019}.
CARBOHYD 70 70 O-linked (DADDGlc) serine.
{ECO:0000269|PubMed:10048019,
ECO:0000269|PubMed:16949362,
ECO:0000269|PubMed:7477282}.
DISULFID 128 158 {ECO:0000269|PubMed:6143785}.
MUTAGEN 75 75 S->A: Alters the morphology of fibers.
{ECO:0000269|PubMed:10048019}.
CONFLICT 161 162 NF -> KAS (in Ref. 1, 2, 3, 4 and 6).
{ECO:0000305}.
HELIX 10 27 {ECO:0000244|PDB:2HI2}.
TURN 28 30 {ECO:0000244|PDB:2HI2}.
HELIX 31 47 {ECO:0000244|PDB:2HI2}.
HELIX 51 61 {ECO:0000244|PDB:2HI2}.
HELIX 68 71 {ECO:0000244|PDB:2HI2}.
HELIX 77 79 {ECO:0000244|PDB:2HI2}.
STRAND 83 91 {ECO:0000244|PDB:2HI2}.
STRAND 94 99 {ECO:0000244|PDB:2HI2}.
STRAND 101 104 {ECO:0000244|PDB:2HI2}.
STRAND 106 108 {ECO:0000244|PDB:2HI2}.
STRAND 112 119 {ECO:0000244|PDB:2HI2}.
STRAND 121 130 {ECO:0000244|PDB:2HI2}.
STRAND 132 136 {ECO:0000244|PDB:2HI2}.
STRAND 139 142 {ECO:0000244|PDB:2HI2}.
HELIX 151 153 {ECO:0000244|PDB:2HI2}.
STRAND 156 158 {ECO:0000244|PDB:2HI2}.
SEQUENCE 165 AA; 17944 MW; BCD3723C11AF5B4C CRC64;
MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ KSAVTEYYLN
HGKWPENNTS AGVASPPSDI KGKYVKEVEV KNGVVTATML SSGVNNEIKG KKLSLWARRE
NGSVKWFCGQ PVTRTDDDTV ADAKDGKEID TKHLPSTCRD NFDAK


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