ID   PIL4_ECOLX              Reviewed;         120 AA.
AC   P10513;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=traA;
OS   Escherichia coli.
OG   Plasmid IncFII R1-19 (R1 drd-19).
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].
RX   PubMed=2564189; DOI=10.1093/nar/17.4.1283;
RA   Koraimann G.M., Hoegenauer G.;
RT   "A stable core region of the tra operon mRNA of plasmid R1-19.";
RL   Nucleic Acids Res. 17:1283-1298(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX   PubMed=3009392; DOI=10.1128/jb.166.2.368-374.1986;
RA   Finlay B.B., Frost L.S., Paranchych W.;
RT   "Nucleotide sequences of the R1-19 plasmid transfer genes traM, finP, traJ,
RT   and traY and the traYZ promoter.";
RL   J. Bacteriol. 166:368-374(1986).
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; K03091; AAA92756.1; -; Genomic_DNA.
DR   EMBL; X13681; CAA31973.1; -; Genomic_DNA.
DR   EMBL; M19710; AAA92659.1; -; Genomic_DNA.
DR   PIR; C23106; YQECR9.
DR   RefSeq; WP_001098998.1; NZ_WWEV01000072.1.
DR   RefSeq; YP_003108302.1; NC_013122.1.
DR   AlphaFoldDB; P10513; -.
DR   SMR; P10513; -.
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_0000024490"
FT   CHAIN           52..120
FT                   /note="Pilin"
FT                   /id="PRO_0000024491"
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..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         52
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   120 AA;  12824 MW;  244800FE8D4DEB2C CRC64;
     MNTVLSVQGA SAPVKKKSFF SKFTRLNMLR LARAVIPAAV LMMFFPQLAM AAQGQDLMAS
     GNTTVKATFG KDSSVVKWVV LAEVLVGAVM YMMTKNVKFL AGFAIISVFI AVGMAVVGLK