FMPA_PSEAI
ID FMPA_PSEAI Reviewed; 150 AA.
AC P02973; Q53390;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 117.
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=PAK;
RX PubMed=2985436; DOI=10.1016/0014-5793(85)80821-8;
RA Pasloske B.L., Finlay B.B., Paranchych W.;
RT "Cloning and sequencing of the Pseudomonas aeruginosa PAK pilin gene.";
RL FEBS Lett. 183:408-412(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAK;
RX PubMed=2430961; DOI=10.1016/s0021-9258(18)66774-2;
RA Johnson K., Parker M.L., Lory S.;
RT "Nucleotide sequence and transcriptional initiation site of two Pseudomonas
RT aeruginosa pilin genes.";
RL J. Biol. Chem. 261:15703-15708(1986).
RN [3]
RP PROTEIN SEQUENCE OF 7-150, AND METHYLATION AT PHE-7.
RC STRAIN=PAK;
RX PubMed=6131838; DOI=10.1016/0014-5793(83)80080-5;
RA Sastry P.A., Pearlstone J.R., Smillie L.B., Paranchych W.;
RT "Amino acid sequence of pilin isolated from Pseudomonas aeruginosa PAK.";
RL FEBS Lett. 151:253-256(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-150.
RX PubMed=7903973; DOI=10.1093/infdis/169.1.134;
RG International Pseudomonas aeruginosa typing study group;
RT "A multicenter comparison of methods for typing strains of Pseudomonas
RT aeruginosa predominantly from patients with cystic fibrosis.";
RL J. Infect. Dis. 169:134-142(1994).
RN [5]
RP STRUCTURE BY NMR OF 134-150.
RX PubMed=8257679; DOI=10.1021/bi00212a008;
RA McInnes C., Soennichsen F.D., Kay C.M., Hodges R.S., Sykes B.D.;
RT "NMR solution structure and flexibility of a peptide antigen representing
RT the receptor binding domain of Pseudomonas aeruginosa.";
RL Biochemistry 32:13432-13440(1993).
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; M14849; AAA25955.1; -; Genomic_DNA.
DR EMBL; X02402; CAA26248.1; -; Genomic_DNA.
DR EMBL; S67807; AAM26730.1; -; Genomic_DNA.
DR PIR; A24603; YQPSPA.
DR RefSeq; WP_058135760.1; NZ_LLUB01000003.1.
DR PDB; 1DZO; X-ray; 1.63 A; A=35-150.
DR PDB; 1NIL; NMR; -; A=134-149.
DR PDB; 1NIM; NMR; -; A=134-149.
DR PDB; 1OQW; X-ray; 2.00 A; A/B=7-150.
DR PDB; 1PAJ; NMR; -; A=134-149.
DR PDB; 1PAK; NMR; -; A=134-149.
DR PDB; 1X6P; X-ray; 1.63 A; A=35-150.
DR PDB; 1X6Q; X-ray; 1.51 A; A=35-150.
DR PDB; 1X6R; X-ray; 1.82 A; A=35-150.
DR PDB; 1X6X; X-ray; 0.96 A; X=35-150.
DR PDB; 1X6Y; X-ray; 1.55 A; A=35-150.
DR PDB; 1X6Z; X-ray; 0.78 A; A=35-150.
DR PDB; 2PY0; X-ray; 1.35 A; A=35-149.
DR PDB; 5VXY; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U=7-150.
DR PDBsum; 1DZO; -.
DR PDBsum; 1NIL; -.
DR PDBsum; 1NIM; -.
DR PDBsum; 1OQW; -.
DR PDBsum; 1PAJ; -.
DR PDBsum; 1PAK; -.
DR PDBsum; 1X6P; -.
DR PDBsum; 1X6Q; -.
DR PDBsum; 1X6R; -.
DR PDBsum; 1X6X; -.
DR PDBsum; 1X6Y; -.
DR PDBsum; 1X6Z; -.
DR PDBsum; 2PY0; -.
DR PDBsum; 5VXY; -.
DR AlphaFoldDB; P02973; -.
DR SMR; P02973; -.
DR IntAct; P02973; 1.
DR iPTMnet; P02973; -.
DR EvolutionaryTrace; P02973; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Fimbrium;
KW Membrane; Methylation; Transmembrane; Transmembrane helix.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:6131838"
FT /id="PRO_0000024176"
FT CHAIN 7..150
FT /note="Fimbrial protein"
FT /id="PRO_0000024177"
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 ECO:0000269|PubMed:6131838"
FT DISULFID 135..148
FT CONFLICT 90
FT /note="T -> TS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101..103
FT /note="TAD -> DTA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> D (in Ref. 4; AAM26730)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="R -> K (in Ref. 2; AAA25955)"
FT /evidence="ECO:0000305"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1X6Z"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:1X6Z"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1X6Z"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1X6Z"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1X6Z"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:1X6Z"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1X6Z"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1X6Z"
FT TURN 115..119
FT /evidence="ECO:0007829|PDB:1X6Z"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1X6Z"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1X6Z"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1X6Z"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1X6Z"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1PAJ"
SQ SEQUENCE 150 AA; 15650 MW; C0E35B69FD6FBE84 CRC64;
MKAQKGFTLI ELMIVVAIIG ILAAIAIPQY QNYVARSEGA SALASVNPLK TTVEEALSRG
WSVKSGTGTE DATKKEVPLG VAADANKLGT IALKPDPADG TADITLTFTM GGAGPKNKGK
IITLTRTAAD GLWKCTSDQD EQFIPKGCSR
