ID   PIL1_SALTI              Reviewed;         119 AA.
AC   P12060;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=traA;
OS   Salmonella typhi.
OG   Plasmid IncFV pED208.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2877970; DOI=10.1128/jb.168.2.990-998.1986;
RA   Finlay B.B., Frost L.S., Paranchych W.;
RT   "Nucleotide sequence of the tra YALE region from IncFV plasmid pED208.";
RL   J. Bacteriol. 168:990-998(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 56-67, AND ACETYLATION AT THR-56.
RX   PubMed=6130062; DOI=10.1128/jb.153.2.950-954.1983;
RA   Frost L.S., Armstrong G.D., Finlay B.B., Edwards B.F.P., Paranchych W.;
RT   "N-terminal amino acid sequencing of EDP208 conjugative pili.";
RL   J. Bacteriol. 153:950-954(1983).
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; M14733; AAA25607.1; -; Genomic_DNA.
DR   PDB; 5LEG; EM; 3.60 A; 1A/1B/1C/1D/1E/1F/1G/1H/1I/1J/1K/1L/1M/1N/1O/1P/2A/2B/2C/2D/2E/2F/2G/2H/2I/2J/2K/2L/2M/2N=57-119.
DR   PDBsum; 5LEG; -.
DR   AlphaFoldDB; P12060; -.
DR   SMR; P12060; -.
DR   iPTMnet; P12060; -.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell inner membrane; Cell membrane; Conjugation;
KW   Direct protein sequencing; Membrane; Plasmid; Secreted; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..55
FT                   /note="Leader peptide; cleaved by LepB"
FT                   /evidence="ECO:0000269|PubMed:6130062"
FT                   /id="PRO_0000024498"
FT   CHAIN           56..119
FT                   /note="Pilin"
FT                   /id="PRO_0000024499"
FT   TOPO_DOM        1..69
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        98..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         56
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000269|PubMed:6130062"
FT   CONFLICT        65..66
FT                   /note="DV -> VD (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   119 AA;  12688 MW;  565FB6047E60918D CRC64;
     MNLSFAKGGL PAPVKNRAWQ YCQMAWRGVT SKKALSRLAA LSPLLLLGVG QMASATDLLA
     GGKDDVKATF GADSFVMMCI IIAELIVGVA MYIRTKNLLI LLGLVVVIVF TTVGLTFIK