ID   FMK1_PSEAI              Reviewed;         154 AA.
AC   P17836;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Fimbrial protein;
DE   AltName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=pilA; Synonyms=fimA;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K122-4;
RX   PubMed=2841299; DOI=10.1128/jb.170.8.3738-3741.1988;
RA   Pasloske B.L., Sastry P.A., Finlay B.B., Paranchych W.;
RT   "Two unusual pilin sequences from different isolates of Pseudomonas
RT   aeruginosa.";
RL   J. Bacteriol. 170:3738-3741(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=9D2;
RX   PubMed=7507890; DOI=10.1128/iai.62.2.371-376.1994;
RA   Castric P.A., Deal C.D.;
RT   "Differentiation of Pseudomonas aeruginosa pili based on sequence and B-
RT   cell epitope analyses.";
RL   Infect. Immun. 62:371-376(1994).
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   -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
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DR   EMBL; M21652; AAC63060.1; -; Genomic_DNA.
DR   EMBL; S68100; AAC60460.1; -; Genomic_DNA.
DR   PIR; B31105; B31105.
DR   RefSeq; WP_003122079.1; NZ_WXZX01000030.1.
DR   AlphaFoldDB; P17836; -.
DR   SMR; P17836; -.
DR   eggNOG; COG4969; Bacteria.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR   InterPro; IPR000983; Bac_GSPG_pilin.
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   PRINTS; PR00813; BCTERIALGSPG.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Fimbrium; Membrane; Methylation; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..6
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024172"
FT   CHAIN           7..154
FT                   /note="Fimbrial protein"
FT                   /id="PRO_0000024173"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         7
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT   DISULFID        133..151
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   154 AA;  16278 MW;  807409FABCC66AD0 CRC64;
     MKAQKGFTLI ELMIVVAIIG ILAAIAIPQY QDYTARTQVT RAVSEVSALK TAAESAILEG
     KEIVSSATPK DTQYDIGFTE STLLDGSGKS QIQVTDNKDG TVELVATLGK SSGSAIKGAV
     ITVSRKNDGV WNCKITKTPT AWKPNYAPAN CPKS