ID   PIL2_ECOLX              Reviewed;         121 AA.
AC   B1VC86;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=traA; ORFNames=IPF_325;
OS   Escherichia coli.
OG   Plasmid pIP1206.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18458128; DOI=10.1128/aac.01540-07;
RA   Perichon B., Bogaerts P., Lambert T., Frangeul L., Courvalin P.,
RA   Galimand M.;
RT   "Sequence of conjugative plasmid pIP1206 mediating resistance to
RT   aminoglycosides by 16S rRNA methylation and to hydrophilic fluoroquinolones
RT   by efflux.";
RL   Antimicrob. Agents Chemother. 52:2581-2592(2008).
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; AM886293; CAP07708.1; -; Genomic_DNA.
DR   RefSeq; WP_000340282.1; NZ_WVUZ01000023.1.
DR   RefSeq; YP_001816522.1; NC_010558.1.
DR   AlphaFoldDB; B1VC86; -.
DR   SMR; B1VC86; -.
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_0000372483"
FT   CHAIN           52..121
FT                   /note="Pilin"
FT                   /id="PRO_0000372484"
FT   TOPO_DOM        1..75
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..100
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         52
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   121 AA;  12798 MW;  C2DF878AB50060E6 CRC64;
     MDAVLSVQGV SAPVKKKSFF SKFTRLNMLR LARAVIPAAV LMMFFPQLAM AAGSSGQDLM
     ASGNTTVKAT FGKDSSVVKW VVLAEVLVGA VMYMMTKNVK FLAGFAIISV FIAVGMAVVG
     L