FMCD_PSEAI
ID FMCD_PSEAI Reviewed; 150 AA.
AC P17837;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=CD;
RX PubMed=2893774; DOI=10.1128/iai.56.3.665-672.1988;
RA Pasloske B.L., Joffe A.M., Sun Q., Volpel K., Paranchych W., Eftekhar F.,
RA Speert D.P.;
RT "Serial isolates of Pseudomonas aeruginosa from a cystic fibrosis patient
RT have identical pilin sequences.";
RL Infect. Immun. 56:665-672(1988).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25945.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M24281; AAA25945.1; ALT_INIT; Genomic_DNA.
DR PIR; A43504; A43504.
DR RefSeq; WP_031636800.1; NZ_VZIL01000044.1.
DR AlphaFoldDB; P17837; -.
DR SMR; P17837; -.
DR PATRIC; fig|287.1494.peg.5534; -.
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:InterPro.
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 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_0000024168"
FT CHAIN 7..150
FT /note="Fimbrial protein"
FT /id="PRO_0000024169"
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 134..147
FT /evidence="ECO:0000250"
SQ SEQUENCE 150 AA; 15743 MW; E14316996F270F3C CRC64;
MKAQKGFTLI ELMIVVAIIG ILAAIAIPQY QNYVARSEGA SALATINPLK TTVEESLSRG
IAGSKILIGT TASTADTTYV GIDEKANKLG TVAVTIKDTG DGTVKFTFAT GQSSPKNAGK
EITLNRTAEG VWTCTSTQEE MFIPKGCNKP