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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
 
 
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