ID   FM12_PSEAI              Reviewed;         154 AA.
AC   P18774;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=1244;
RX   PubMed=2499765; DOI=10.1007/bf00332233;
RA   Castric P.A., Sidberry H.F., Sadoff J.C.;
RT   "Cloning and sequencing of the Pseudomonas aeruginosa 1244 pilin structural
RT   gene.";
RL   Mol. Gen. Genet. 216:75-80(1989).
RN   [2]
RP   STRUCTURE OF O-LINKED CARBOHYDRATE.
RC   STRAIN=1244;
RX   PubMed=11342554; DOI=10.1074/jbc.m102685200;
RA   Castric P., Cassels F.J., Carlson R.W.;
RT   "Structural characterization of the Pseudomonas aeruginosa 1244 pilin
RT   glycan.";
RL   J. Biol. Chem. 276:26479-26485(2001).
RN   [3]
RP   GLYCOSYLATION AT SER-154, AND MUTAGENESIS OF SER-154.
RC   STRAIN=1244;
RX   PubMed=12010970; DOI=10.1128/iai.70.6.2837-2845.2002;
RA   Comer J.E., Marshall M.A., Blanch V.J., Deal C.D., Castric P.;
RT   "Identification of the Pseudomonas aeruginosa 1244 pilin glycosylation
RT   site.";
RL   Infect. Immun. 70:2837-2845(2002).
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: O-glycosylated; glycan consists of 5NbetaOHC47NFmPse(alpha2-
CC       4)Xyl(beta1-3)FucNAc in beta1-O linkage to Ser.
CC       {ECO:0000269|PubMed:12010970}.
CC   -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
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DR   EMBL; X83916; CAA58768.1; -; Genomic_DNA.
DR   PIR; S04440; S04440.
DR   RefSeq; WP_058150672.1; NZ_WUDG01000018.1.
DR   PDB; 6BBK; X-ray; 1.73 A; A=34-154.
DR   PDBsum; 6BBK; -.
DR   AlphaFoldDB; P18774; -.
DR   SMR; P18774; -.
DR   GlyConnect; 163; 1 O-Linked glycan.
DR   iPTMnet; P18774; -.
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   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Fimbrium; Glycoprotein; Membrane;
KW   Methylation; Transmembrane; Transmembrane helix.
FT   PROPEP          1..6
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024166"
FT   CHAIN           7..154
FT                   /note="Fimbrial protein"
FT                   /id="PRO_0000024167"
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   CARBOHYD        154
FT                   /note="O-linked (FucNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:12010970"
FT   DISULFID        133..151
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         154
FT                   /note="S->A: Loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:12010970"
FT   HELIX           34..47
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   HELIX           50..59
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   HELIX           88..91
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   STRAND          102..108
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   TURN            114..118
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   STRAND          131..137
FT                   /evidence="ECO:0007829|PDB:6BBK"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:6BBK"
SQ   SEQUENCE   154 AA;  16278 MW;  9A6E09E0A6C66AD0 CRC64;
     MKAQKGFTLI ELMIVVAIIG ILAAIAIPQY QDYTARTQVT RAVSEVSALK TAAESAILEG
     KEIVSSATPK DTQYDIGFTE STLLDGSGKS QIQVTDNQDG TVELVATLGK SSGSAIKGAV
     ITVSRKNDGV WNCKITKTPT AWKPNYAPAN CPKS