PIL7_ECOLX
ID PIL7_ECOLX Reviewed; 119 AA.
AC P14496;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Pilin;
DE Flags: Precursor;
GN Name=traA;
OS Escherichia coli.
OG Plasmid IncFII ColB2.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6090427; DOI=10.1128/jb.160.1.402-407.1984;
RA Finlay B.B., Frost L.S., Paranchych W.;
RT "Localization, cloning, and sequence determination of the conjugative
RT plasmid ColB2 pilin gene.";
RL J. Bacteriol. 160:402-407(1984).
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; K02667; AAB05355.1; -; Genomic_DNA.
DR PIR; I40630; I40630.
DR AlphaFoldDB; P14496; -.
DR SMR; P14496; -.
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_0000024496"
FT CHAIN 52..119
FT /note="Pilin"
FT /id="PRO_0000024497"
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; 12707 MW; D800EB8D424186C4 CRC64;
MNAVLSVQGA SAPVKKKSFF SKFTRLNMLR LARAVIPAAV LMMFFPQLAM AAQGQDLMAS
GNTTVKATFG KDSSVVKWVV LAEVLVGAVM YMMTKNVKFL AGFAIISVFI AVVMAVVGL