ID   PIL6_ECOLX              Reviewed;         119 AA.
AC   P14495;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=traA;
OS   Escherichia coli.
OG   Plasmid ColB4, Plasmid ColB2-like, Plasmid IncFIV R124, and
OG   Plasmid IncFII R538.
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).
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; K03093; AAA92760.1; -; Genomic_DNA.
DR   EMBL; K03085; AAA23012.1; -; Genomic_DNA.
DR   PIR; B23106; YQECB2.
DR   RefSeq; WP_000994781.1; NZ_WVVH01000037.1.
DR   AlphaFoldDB; P14495; -.
DR   SMR; P14495; -.
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                   /id="PRO_0000024494"
FT   CHAIN           52..119
FT                   /note="Pilin"
FT                   /id="PRO_0000024495"
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;  12665 MW;  D800EB8D42419C74 CRC64;
     MNAVLSVQGA SAPVKKKSFF SKFTRLNMLR LARAVIPAAV LMMFFPQLAM AAQGQDLMAS
     GNTTVKATFG KDSSVVKWVV LAEVLVGAVM YMMTKNVKFL AGFAIISVFI AVGMAVVGL