FMM1_NEIGO
ID FMM1_NEIGO Reviewed; 165 AA.
AC P02974;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Type IV major pilin protein PilE1;
DE AltName: Full=MS11 antigen;
DE AltName: Full=Pilin;
DE Flags: Precursor;
GN Name=pilE1;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MS11;
RX PubMed=6148752; DOI=10.1073/pnas.81.19.6110;
RA Meyer T.F., Billyard E., Haas R., Storzbach S., So M.;
RT "Pilus genes of Neisseria gonorrheae: chromosomal organization and DNA
RT sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6110-6114(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2872674; DOI=10.1073/pnas.83.11.3890;
RA Bergstroem S., Robbins K., Koomey J.M., Swanson J.;
RT "Piliation control mechanisms in Neisseria gonorrhoeae.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3890-3894(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1671354; DOI=10.1002/j.1460-2075.1991.tb07970.x;
RA Jonsson A.B., Nyberg G., Normark S.;
RT "Phase variation of gonococcal pili by frameshift mutation in pilC, a novel
RT gene for pilus assembly.";
RL EMBO J. 10:477-488(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1348857; DOI=10.1073/pnas.89.8.3204;
RA Jonsson A.B., Pfeifer J., Normark S.;
RT "Neisseria gonorrhoeae PilC expression provides a selective mechanism for
RT structural diversity of pili.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3204-3208(1992).
RN [5]
RP PROTEIN SEQUENCE OF 8-36, AND METHYLATION AT PHE-8.
RC STRAIN=33, 7122, ATCC 33084 / F62 / M-1914, and B;
RX PubMed=413571; DOI=10.1021/bi00596a010;
RA Hermodson M.A., Chen K.C., Buchanan T.M.;
RT "Neisseria pili proteins: amino-terminal amino acid sequences and
RT identification of an unusual amino acid.";
RL Biochemistry 17:442-445(1978).
RN [6]
RP PROTEIN SEQUENCE OF 8-165, AND PRESENCE OF PHOSPHORYLATION.
RC STRAIN=MS11;
RX PubMed=6143785; DOI=10.1084/jem.159.5.1351;
RA Schoolnik G.K., Fernandez R., Tai J.Y., Rothbard J., Gotschlich E.C.;
RT "Gonococcal pili. Primary structure and receptor binding domain.";
RL J. Exp. Med. 159:1351-1370(1984).
RN [7]
RP PHOSPHORYLATION AT SER-75.
RC STRAIN=MS11;
RX PubMed=15249686; DOI=10.1073/pnas.0402397101;
RA Hegge F.T., Hitchen P.G., Aas F.E., Kristiansen H., Lovold C.,
RA Egge-Jacobsen W., Panico M., Leong W.Y., Bull V., Virji M., Morris H.R.,
RA Dell A., Koomey M.;
RT "Unique modifications with phosphocholine and phosphoethanolamine define
RT alternate antigenic forms of Neisseria gonorrhoeae type IV pili.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10798-10803(2004).
RN [8]
RP PHOSPHORYLATION AT SER-75.
RC STRAIN=MS11;
RX PubMed=16825186; DOI=10.1074/jbc.m604324200;
RA Aas F.E., Egge-Jacobsen W., Winther-Larsen H.C., Lovold C., Hitchen P.G.,
RA Dell A., Koomey M.;
RT "Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical
RT modifications with phosphoethanolamine and phosphocholine requiring an
RT enzyme structurally related to lipopolysaccharide phosphoethanolamine
RT transferases.";
RL J. Biol. Chem. 281:27712-27723(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21615661; DOI=10.1111/j.1462-5822.2011.01607.x;
RA Dietrich M., Bartfeld S., Munke R., Lange C., Ogilvie L.A., Friedrich A.,
RA Meyer T.F.;
RT "Activation of NF-kappaB by Neisseria gonorrhoeae is associated with
RT microcolony formation and type IV pilus retraction.";
RL Cell. Microbiol. 13:1168-1182(2011).
RN [10]
RP FUNCTION, REGION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-128.
RX PubMed=27213957; DOI=10.1371/journal.pgen.1006069;
RA Obergfell K.P., Seifert H.S.;
RT "The Pilin N-terminal Domain Maintains Neisseria gonorrhoeae Transformation
RT Competence during Pilus Phase Variation.";
RL PLoS Genet. 12:e1006069-e1006069(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 8-165, METHYLATION AT PHE-8,
RP GLYCOSYLATION AT SER-70, AND SEQUENCE REVISION TO C-TERMINUS.
RC STRAIN=MS11;
RX PubMed=7477282; DOI=10.1038/378032a0;
RA Parge H.E., Forest K.T., Hickey M.J., Christensen D.A., Getzoff E.,
RA Tainer J.A.;
RT "Structure of the fibre-forming protein pilin at 2.6-A resolution.";
RL Nature 378:32-38(1995).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 8-165, PHOSPHORYLATION AT SER-75,
RP GLYCOSYLATION AT SER-70, PHOSPHORYLATION AT SER-101, MUTAGENESIS OF SER-75,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=MS11;
RX PubMed=10048019; DOI=10.1046/j.1365-2958.1999.01184.x;
RA Forest K.T., Dunham S.A., Koomey M., Tainer J.A.;
RT "Crystallographic structure reveals phosphorylated pilin from Neisseria:
RT phosphoserine sites modify type IV pilus surface chemistry and fibre
RT morphology.";
RL Mol. Microbiol. 31:743-752(1999).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.5 ANGSTROMS), GLYCOSYLATION AT SER-70,
RP AND X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 8-165.
RC STRAIN=MS11;
RX PubMed=16949362; DOI=10.1016/j.molcel.2006.07.004;
RA Craig L., Volkmann N., Arvai A.S., Pique M.E., Yeager M., Egelman E.H.,
RA Tainer J.A.;
RT "Type IV pilus structure by cryo-electron microscopy and crystallography:
RT implications for pilus assembly and functions.";
RL Mol. Cell 23:651-662(2006).
CC -!- FUNCTION: Major component of the type IV pilus (T4P) that plays a role
CC in cellular adherence, microcolony formation, resistance to neutrophil
CC mediated killing, twitching motility as well as transformation
CC (PubMed:27213957). Mediates the attachment and the formation of
CC bacterial microcolonies on host epithelial cells. Mechanistically, pili
CC retractation induces host NF-kappa-B activation in infected cells,
CC which is temporally associated with the formation of gonococcal
CC microcolonies (PubMed:27213957). {ECO:0000269|PubMed:27213957}.
CC -!- SUBUNIT: The pili are polar flexible filaments of about 5.4 nanometers
CC diameter and 2.5 micrometers average length; they consist of only a
CC single polypeptide chain arranged in a helical configuration of five
CC subunits per turn in the assembled pilus.
CC -!- SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- PTM: The O-linked glycan identified as Gal-GlcNAc disaccharide in
CC PubMed:7477282 and PubMed:10048019 is now identified as either a
CC hexosyl-diacetamidotrideoxyhexoside (DATDHex) by mass spectrometry in
CC PubMed:15249686, or alpha-D-galactopyranosyl-(1->3)-2,4-diacetamido-
CC 2,4-dideoxy-beta-D-glucopyranoside (DADDGlc) by X-ray diffraction in
CC PubMed:16949362. It is not clear whether there is a chemical difference
CC in the glycosylation of the two derivatives of strain MS11 used in
CC these experiments, or not. {ECO:0000269|PubMed:10048019,
CC ECO:0000269|PubMed:7477282}.
CC -!- PTM: In some MS11 derivative strains, Ser-75 is modified to O-(2-
CC aminoethylphosphoryl)serine, and in some other derivatives that can be
CC secondarily modified to O-(2-cholinephosphoryl)serine by N-methylation.
CC {ECO:0000269|PubMed:413571, ECO:0000269|PubMed:7477282}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants show a complete absence of
CC observable pili. {ECO:0000269|PubMed:27213957}.
CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
CC -!- CAUTION: In PubMed:413571 it is said that 50% of the peptides have N-
CC methyl-Phe and 50% begin with Thr-9. N-terminal methylation produces
CC preview during Edman degradation, which makes this appear to happen
CC when the peptide is completely N-terminal methylated. {ECO:0000305}.
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DR EMBL; K02078; AAA25466.1; -; Genomic_DNA.
DR EMBL; M13222; AAA25468.1; -; mRNA.
DR PIR; A94007; YQNHG.
DR PDB; 1AY2; X-ray; 2.60 A; A=9-165.
DR PDB; 2HI2; X-ray; 2.30 A; A=8-165.
DR 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.
DR PDB; 2PIL; X-ray; 2.60 A; A=8-165.
DR PDB; 5VXX; EM; 5.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U=8-165.
DR PDBsum; 1AY2; -.
DR PDBsum; 2HI2; -.
DR PDBsum; 2HIL; -.
DR PDBsum; 2PIL; -.
DR PDBsum; 5VXX; -.
DR AlphaFoldDB; P02974; -.
DR SMR; P02974; -.
DR DrugBank; DB04522; Dexfosfoserine.
DR DrugBank; DB04079; Heptane-1,2,3-Triol.
DR DrugBank; DB06838; methyl L-phenylalaninate.
DR iPTMnet; P02974; -.
DR EvolutionaryTrace; P02974; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR001082; Pilin.
DR InterPro; IPR045584; Pilin-like.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF00114; Pilin; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Fimbrium; Glycoprotein; Membrane; Methylation; Phosphoprotein;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..7
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:413571, ECO:0000269|PubMed:6143785"
FT /id="PRO_0000024154"
FT CHAIN 8..165
FT /note="Type IV major pilin protein PilE1"
FT /id="PRO_0000024155"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 137..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:413571, ECO:0000269|PubMed:6143785,
FT ECO:0000269|PubMed:7477282"
FT MOD_RES 75
FT /note="O-(2-aminoethylphosphoryl)serine; alternate"
FT /evidence="ECO:0000269|PubMed:10048019,
FT ECO:0000269|PubMed:15249686, ECO:0000269|PubMed:16825186"
FT MOD_RES 75
FT /note="O-(2-cholinephosphoryl)serine; alternate"
FT /evidence="ECO:0000269|PubMed:10048019,
FT ECO:0000269|PubMed:15249686, ECO:0000269|PubMed:16825186"
FT MOD_RES 75
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000269|PubMed:10048019,
FT ECO:0000269|PubMed:15249686, ECO:0000269|PubMed:16825186"
FT MOD_RES 101
FT /note="O-(sn-1-glycerophosphoryl)serine; partial"
FT /evidence="ECO:0000269|PubMed:10048019"
FT CARBOHYD 70
FT /note="O-linked (DADDGlc) serine"
FT /evidence="ECO:0000269|PubMed:10048019,
FT ECO:0000269|PubMed:16949362, ECO:0000269|PubMed:7477282"
FT DISULFID 128..158
FT /evidence="ECO:0000269|PubMed:6143785"
FT MUTAGEN 75
FT /note="S->A: Alters the morphology of fibers."
FT /evidence="ECO:0000269|PubMed:10048019"
FT MUTAGEN 128
FT /note="C->G: Loss of pili."
FT /evidence="ECO:0000269|PubMed:27213957"
FT CONFLICT 161..162
FT /note="NF -> KAS (in Ref. 1, 2, 3, 4 and 6)"
FT /evidence="ECO:0000305"
FT HELIX 10..27
FT /evidence="ECO:0007829|PDB:2HI2"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2HI2"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:2HI2"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2HI2"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2HI2"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2HI2"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2HI2"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2HI2"
SQ SEQUENCE 165 AA; 17944 MW; BCD3723C11AF5B4C CRC64;
MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ KSAVTEYYLN
HGKWPENNTS AGVASPPSDI KGKYVKEVEV KNGVVTATML SSGVNNEIKG KKLSLWARRE
NGSVKWFCGQ PVTRTDDDTV ADAKDGKEID TKHLPSTCRD NFDAK
