ID   FMP1_PSEAI              Reviewed;         157 AA.
AC   P17838;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=P1;
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   STRUCTURE BY NMR OF 36-157.
RX   PubMed=11294863; DOI=10.1074/jbc.m100659200;
RA   Keizer D.W., Slupsky C.M., Kalisiak M., Campbell A.P., Crump M.P.,
RA   Sastry P.A., Hazes B., Irvin R.T., Sykes B.D.;
RT   "Structure of a pilin monomer from Pseudomonas aeruginosa: implications for
RT   the assembly of pili.";
RL   J. Biol. Chem. 276:24186-24193(2001).
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; M21651; AAC63062.1; -; Genomic_DNA.
DR   PIR; A31105; A31105.
DR   PDB; 1HPW; NMR; -; A=36-157.
DR   PDB; 1QVE; X-ray; 1.54 A; A/B=36-157.
DR   PDB; 1RG0; X-ray; 1.80 A; A/B=36-157.
DR   PDBsum; 1HPW; -.
DR   PDBsum; 1QVE; -.
DR   PDBsum; 1RG0; -.
DR   AlphaFoldDB; P17838; -.
DR   SMR; P17838; -.
DR   EvolutionaryTrace; P17838; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IMP:CAFA.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043208; F:glycosphingolipid binding; IMP:CAFA.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IMP:CAFA.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   DisProt; DP00206; -.
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; Disulfide bond; Fimbrium; Membrane; Methylation;
KW   Transmembrane; Transmembrane helix.
FT   PROPEP          1..7
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024170"
FT   CHAIN           8..157
FT                   /note="Fimbrial protein"
FT                   /id="PRO_0000024171"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         8
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT   DISULFID        64..100
FT   DISULFID        136..149
FT   HELIX           36..48
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:1HPW"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   STRAND          83..95
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   STRAND          98..106
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   TURN            127..129
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   STRAND          133..140
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:1QVE"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:1QVE"
SQ   SEQUENCE   157 AA;  16176 MW;  234E3FB1D5C1EA49 CRC64;
     MKAAQKGFTL IELMIVVAII GILAAIAIPA YQDYTARAQL SERMTLASGL KTKVSDIFSQ
     DGSCPANTAA TAGIEKDTDI NGKYVAKVTT GGTAAASGGC TIVATMKASD VATPLRGKTL
     TLTLGNADKG SYTWACTSNA DNKYLPKTCQ TATTTTP