PIL5_ECOLX
ID PIL5_ECOLX Reviewed; 119 AA.
AC P14494;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Pilin;
DE Flags: Precursor;
GN Name=traA;
OS Escherichia coli.
OG Plasmid IncFII R100-1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2999074; DOI=10.1128/jb.164.3.1238-1247.1985;
RA Frost L.S., Finlay B.B., Opgenorth A., Paranchych W., Lee J.S.;
RT "Characterization and sequence analysis of pilin from F-like plasmids.";
RL J. Bacteriol. 164:1238-1247(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=2836369; DOI=10.1128/jb.170.6.2749-2757.1988;
RA Inamoto S., Yoshioka Y., Ohtsubo E.;
RT "Identification and characterization of the products from the traJ and traY
RT genes of plasmid R100.";
RL J. Bacteriol. 170:2749-2757(1988).
CC -!- FUNCTION: Propilin is the precursor of the pilus subunit, pilin, that
CC forms conjugative pili, the filamentous surface appendages required for
CC cell-to-cell contact during the earlier stages of bacterial
CC conjugation, and that retract after contact is established. Mature
CC pilin is assembled with the help of TraQ and TraX (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with itself to form filaments; also
CC interacts with TraQ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC Secreted {ECO:0000250}. Note=Propilin is directed to the inner
CC membrane, where it is cleaved and acetylated. Mature pilin forms
CC filaments that are secreted to form the conjugative pilus (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TraA family. {ECO:0000305}.
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DR EMBL; K03090; AAA92754.1; -; Genomic_DNA.
DR EMBL; M20941; AAA26074.1; -; Genomic_DNA.
DR PIR; D23106; YQECR1.
DR RefSeq; NP_957600.1; NC_005327.1.
DR RefSeq; WP_001098992.1; NZ_WVVN01000094.1.
DR RefSeq; YP_001096468.1; NC_009133.1.
DR RefSeq; YP_002456188.1; NC_011812.1.
DR RefSeq; YP_003108228.1; NC_013121.1.
DR RefSeq; YP_006952238.1; NC_019057.1.
DR RefSeq; YP_006953322.1; NC_019071.1.
DR RefSeq; YP_006953421.1; NC_019072.1.
DR RefSeq; YP_006953948.1; NC_019090.1.
DR RefSeq; YP_006954269.1; NC_019095.1.
DR RefSeq; YP_006990760.1; NC_019424.1.
DR RefSeq; YP_007447546.1; NC_020278.2.
DR AlphaFoldDB; P14494; -.
DR SMR; P14494; -.
DR GeneID; 58462408; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR008873; TraA.
DR Pfam; PF05513; TraA; 1.
DR TIGRFAMs; TIGR02758; TraA_TIGR; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell inner membrane; Cell membrane; Conjugation; Membrane;
KW Plasmid; Secreted; Transmembrane; Transmembrane helix.
FT PROPEP 1..51
FT /note="Leader peptide; cleaved by LepB"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024492"
FT CHAIN 52..119
FT /note="Pilin"
FT /id="PRO_0000024493"
FT TOPO_DOM 1..73
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 52
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 119 AA; 12762 MW; C0FE522616A3E76B CRC64;
MNTVLSVQGA SAPVEKKSFF SKFTRLNMLR LVRAVIPVAV LMMLFPELAM AAGKGDLMAK
GNDTVKATFG KDSSIVKWVV LAEVLVGAVM YMMTKNVKFL VGFAIISVFI AVGMSVVGL