PIL1_ECOLI
ID PIL1_ECOLI Reviewed; 121 AA.
AC P04737; P14517;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Pilin;
DE AltName: Full=F-pilin;
DE Flags: Precursor;
GN Name=traA; OrderedLocusNames=ECOK12F074;
OS Escherichia coli (strain K12).
OG Plasmid F, Plasmid IncFI R386, Plasmid IncFI ColV2-K94, and
OG Plasmid IncFI ColVBtrp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 52-59, ACETYLATION
RP AT ALA-52, AND FUNCTION.
RC PLASMID=F;
RX PubMed=6090426; DOI=10.1128/jb.160.1.395-401.1984;
RA Frost L.S., Paranchych W., Willetts N.S.;
RT "DNA sequence of the F traALE region that includes the gene for F pilin.";
RL J. Bacteriol. 160:395-401(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=F;
RX PubMed=7915817; DOI=10.1128/mr.58.2.162-210.1994;
RA Frost L.S., Ippen-Ihler K., Skurray R.A.;
RT "Analysis of the sequence and gene products of the transfer region of the F
RT sex factor.";
RL Microbiol. Rev. 58:162-210(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncFI ColV2-K94, IncFI ColVBtrp, and IncFI R386;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / CR63; PLASMID=F;
RA Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
RT "Complete nucleotide sequence of the F plasmid: its implications for
RT organization and diversification of plasmid genomes.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP BACTERIOPHAGE ATTACHMENT TO PILIN, AND MUTAGENESIS OF GLY-9; PRO-13;
RP LYS-68; LYS-73; VAL-81 AND GLY-120.
RX PubMed=2906110; DOI=10.1007/bf00333409;
RA Frost L.S., Paranchych W.;
RT "DNA sequence analysis of point mutations in traA, the F pilin gene, reveal
RT two domains involved in F-specific bacteriophage attachment.";
RL Mol. Gen. Genet. 213:134-139(1988).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TOPOLOGY.
RC PLASMID=F;
RX PubMed=1464628; DOI=10.1016/s0021-9258(18)35734-x;
RA Paiva W.D., Grossman T., Silverman P.M.;
RT "Characterization of F-pilin as an inner membrane component of Escherichia
RT coli K12.";
RL J. Biol. Chem. 267:26191-26197(1992).
RN [7]
RP INTERACTION WITH TRAQ.
RC PLASMID=F;
RX PubMed=8095257; DOI=10.1128/jb.175.5.1384-1391.1993;
RA Maneewannakul K., Maneewannakul S., Ippen-Ihler K.;
RT "Synthesis of F pilin.";
RL J. Bacteriol. 175:1384-1391(1993).
RN [8]
RP CLEAVAGE OF LEADER PEPTIDE BY LEPB.
RC PLASMID=F;
RX PubMed=8682775; DOI=10.1128/jb.178.13.3742-3747.1996;
RA Majdalani N., Ippen-Ihler K.;
RT "Membrane insertion of the F-pilin subunit is Sec independent but requires
RT leader peptidase B and the proton motive force.";
RL J. Bacteriol. 178:3742-3747(1996).
RN [9]
RP MUTAGENESIS OF LEU-121.
RX PubMed=9641980; DOI=10.1006/jmbi.1998.1773;
RA Rondot S., Anthony K.G., Duebel S., Ida N., Wiemann S., Beyreuther K.,
RA Frost L.S., Little M., Breitling F.;
RT "Epitopes fused to F-pilin are incorporated into functional recombinant
RT pili.";
RL J. Mol. Biol. 279:589-603(1998).
RN [10]
RP INTERACTION WITH TRAQ.
RC PLASMID=F;
RX PubMed=10564517; DOI=10.1046/j.1365-2958.1999.01640.x;
RA Harris R.L., Sholl K.A., Conrad M.N., Dresser M.E., Silverman P.M.;
RT "Interaction between the F plasmid TraA (F-pilin) and TraQ proteins.";
RL Mol. Microbiol. 34:780-791(1999).
RN [11]
RP MUTAGENESIS OF ASP-58; LYS-68; ALA-69; PHE-71; GLY-72; LYS-73; ASP-74;
RP LYS-79; GLU-85; TYR-93; LYS-97; ASN-98; VAL-99; LYS-100; PHE-101; PHE-105
RP AND PHE-111.
RC PLASMID=F;
RX PubMed=11849547; DOI=10.1046/j.1365-2958.2002.02731.x;
RA Manchak J., Anthony K.G., Frost L.S.;
RT "Mutational analysis of F-pilin reveals domains for pilus assembly, phage
RT infection and DNA transfer.";
RL Mol. Microbiol. 43:195-205(2002).
RN [12]
RP FUNCTION AS RECEPTOR FOR CDIA-CT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-74 AND GLY-120.
RC STRAIN=K12 / X90; PLASMID=F;
RX PubMed=24889811; DOI=10.1111/mmi.12658;
RA Beck C.M., Diner E.J., Kim J.J., Low D.A., Hayes C.S.;
RT "The F pilus mediates a novel pathway of CDI toxin import.";
RL Mol. Microbiol. 93:276-290(2014).
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 (PubMed:1464628,
CC PubMed:6090426). Functions as a receptor for CdiA-CT from E.cloacae and
CC E.coli, although it is not clear if this is physiologically relevant
CC (PubMed:24889811). {ECO:0000269|PubMed:1464628,
CC ECO:0000269|PubMed:24889811, ECO:0000269|PubMed:6090426}.
CC -!- SUBUNIT: Monomer. Interacts with itself to form filaments; also
CC interacts with TraQ. {ECO:0000269|PubMed:10564517,
CC ECO:0000269|PubMed:1464628, ECO:0000269|PubMed:8095257}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1464628};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1464628}. Secreted
CC {ECO:0000269|PubMed:1464628}. 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.
CC -!- DISRUPTION PHENOTYPE: Loss of sensitivity to toxin CdiA-CT.
CC {ECO:0000269|PubMed:24889811}.
CC -!- SIMILARITY: Belongs to the TraA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K01147; AAA24910.1; -; Genomic_DNA.
DR EMBL; U01159; AAC44177.1; -; Genomic_DNA.
DR EMBL; M11322; AAA98308.1; -; Genomic_DNA.
DR EMBL; AP001918; BAA97944.1; -; Genomic_DNA.
DR EMBL; K03086; AAA92543.1; -; Genomic_DNA.
DR EMBL; K03087; AAA92545.1; -; Genomic_DNA.
DR PIR; A23106; YQECFX.
DR PIR; A29332; YQECF.
DR RefSeq; NP_061453.1; NC_002483.1.
DR RefSeq; NP_862919.1; NC_004998.1.
DR RefSeq; WP_000994779.1; NZ_SSUW01000046.1.
DR RefSeq; YP_003937617.1; NC_014615.1.
DR RefSeq; YP_009060156.1; NC_024956.1.
DR RefSeq; YP_009068351.1; NC_025139.1.
DR RefSeq; YP_009070616.1; NC_025175.1.
DR RefSeq; YP_009071230.1; NC_025179.1.
DR PDB; 5LER; EM; 5.00 A; 1A/1B/1C/1D/1E/1F/1G/1H/1I/1J/1K/1L/1M/1N/1O/2A/2B/2C/2D/2E/2F/2G/2H/2I/2J/2K/2L/2M/2N/2O=57-121.
DR PDB; 5LFB; EM; 5.00 A; 1A/1B/1C/1D/1E/1F/1G/1H/1I/1J/1K/1L/1M/1N/1O/2A/2B/2C/2D/2E/2F/2G/2H/2I/2J/2K/2L/2M/2N/2O=57-121.
DR PDBsum; 5LER; -.
DR PDBsum; 5LFB; -.
DR AlphaFoldDB; P04737; -.
DR SMR; P04737; -.
DR IntAct; P04737; 1.
DR iPTMnet; P04737; -.
DR PRIDE; P04737; -.
DR PATRIC; fig|83333.107.peg.639; -.
DR PRO; PR:P04737; -.
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..51
FT /note="Leader peptide; cleaved by LepB"
FT /evidence="ECO:0000269|PubMed:6090426"
FT /id="PRO_0000024487"
FT CHAIN 52..121
FT /note="Pilin"
FT /id="PRO_0000024488"
FT TOPO_DOM 1..75
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:1464628"
FT TRANSMEM 76..96
FT /note="Helical"
FT TOPO_DOM 97..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1464628"
FT TRANSMEM 101..121
FT /note="Helical"
FT MOD_RES 52
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:6090426"
FT MUTAGEN 9
FT /note="G->S: No production of pili."
FT /evidence="ECO:0000269|PubMed:2906110"
FT MUTAGEN 13
FT /note="P->S: No production of pili."
FT /evidence="ECO:0000269|PubMed:2906110"
FT MUTAGEN 58
FT /note="D->A: No production of propilin or pilin."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 68
FT /note="K->A: No production of propilin or pilin."
FT /evidence="ECO:0000269|PubMed:11849547,
FT ECO:0000269|PubMed:2906110"
FT MUTAGEN 68
FT /note="K->E: Resistant to phage R17 attachment."
FT /evidence="ECO:0000269|PubMed:11849547,
FT ECO:0000269|PubMed:2906110"
FT MUTAGEN 69
FT /note="A->E: No effect on propilin synthesis. No effect on
FT pilus formation. Resistant to phage R17 attachment."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 71
FT /note="F->V: No effect on propilin synthesis. Defective
FT pilus tip assembly."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 72
FT /note="G->D: No effect on propilin synthesis. No effect on
FT pilus formation."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 73
FT /note="K->A,T: No effect on propilin synthesis. No effect
FT on pilus formation."
FT /evidence="ECO:0000269|PubMed:11849547,
FT ECO:0000269|PubMed:2906110"
FT MUTAGEN 74
FT /note="D->G: No effect on propilin synthesis, no effect on
FT pilus formation, resistant to phage R17 attachment
FT (Ref.11). About 67% conjugation efficiency, E.coli still
FT sensitive to CdiA-CT toxin (Ref.12)."
FT /evidence="ECO:0000269|PubMed:11849547,
FT ECO:0000269|PubMed:24889811"
FT MUTAGEN 79
FT /note="K->A: No effect on propilin synthesis. Resistant to
FT phage R17 attachment."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 79
FT /note="K->I: No effect on propilin synthesis. Defective
FT pilus tip assembly."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 81
FT /note="V->I: Slightly reduced phage R17 attachment, reduced
FT ability to retract."
FT /evidence="ECO:0000269|PubMed:2906110"
FT MUTAGEN 85
FT /note="E->A,G: No effect on propilin synthesis. Defective
FT pilus tip assembly."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 93
FT /note="Y->D: Production of small amounts of propilin and
FT pilin."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 97
FT /note="K->A,R,V: No effect on propilin synthesis. No effect
FT on pilus formation. Inability to support R17 phage
FT eclipse."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 97
FT /note="K->A: Reduced cleavage of propilin to pilin; when
FT associated with A-100."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 98
FT /note="N->A: No effect on propilin synthesis. No effect on
FT pilus formation."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 99
FT /note="V->A: No effect on propilin synthesis. No effect on
FT pilus formation. Inability to support R17 phage eclipse."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 100
FT /note="K->A,R,T: No effect on propilin synthesis. No effect
FT on pilus formation. Inability to support R17 phage eclipse.
FT Reduced DNA transfer."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 100
FT /note="K->A: Reduced cleavage of propilin to pilin; when
FT associated with A-97."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 101
FT /note="F->A: No effect on propilin synthesis. No effect on
FT pilus formation. Inability to support R17 phage eclipse.
FT Reduced DNA transfer."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 105
FT /note="F->V: No effect on propilin synthesis. No effect on
FT pilus formation. Inability to support R17 phage eclipse.
FT Reduced DNA transfer."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 111
FT /note="F->V: No effect on propilin synthesis. No effect on
FT pilus formation. Inability to support R17 phage eclipse.
FT Reduced DNA transfer."
FT /evidence="ECO:0000269|PubMed:11849547"
FT MUTAGEN 120
FT /note="G->C: Resistant to phage R17, conjugation normal,
FT provides partial resistance to CdiA-CT toxin."
FT /evidence="ECO:0000269|PubMed:24889811"
FT MUTAGEN 120
FT /note="G->D: Resistant to phages R17 and QB attachment."
FT /evidence="ECO:0000269|PubMed:2906110"
FT MUTAGEN 121
FT /note="L->S: No effect on propilin synthesis. Defective
FT pilus tip assembly."
FT /evidence="ECO:0000269|PubMed:9641980"
FT CONFLICT 115
FT /note="G -> V (in Ref. 1; AAA24910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 121 AA; 12768 MW; C65EEA3C6E7EF2A2 CRC64;
MNAVLSVQGA SAPVKKKSFF SKFTRLNMLR LARAVIPAAV LMMFFPQLAM AAGSSGQDLM
ASGNTTVKAT FGKDSSVVKW VVLAEVLVGA VMYMMTKNVK FLAGFAIISV FIAVGMAVVG
L
