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Protein

Pilin

Gene

traA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Propilin is the precursor of the pilus subunit, pilin, that forms conjugative pili, the filamentous surface appendages required for cell-to-cell contact during the earlier stages of bacterial conjugation, and that retract after contact is established. Mature pilin is assembled with the help of TraQ and TraX (PubMed:1464628, PubMed:6090426). Functions as a receptor for CdiA-CT from E.cloacae and E.coli, although it is not clear if this is physiologically relevant (PubMed:24889811).3 Publications

GO - Biological processi

Keywordsi

Biological processConjugation

Names & Taxonomyi

Protein namesi
Recommended name:
Pilin
Alternative name(s):
F-pilin
Gene namesi
Name:traA
Ordered Locus Names:ECOK12F074
Encoded oniPlasmid F9 Publications
Plasmid IncFI R3861 Publication
Plasmid IncFI ColV2-K941 Publication
Plasmid IncFI ColVBtrp1 Publication
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 75Periplasmic1 PublicationAdd BLAST75
Transmembranei76 – 96HelicalAdd BLAST21
Topological domaini97 – 100Cytoplasmic1 Publication4
Transmembranei101 – 121HelicalAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Loss of sensitivity to toxin CdiA-CT.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9G → S: No production of pili. 1 Publication1
Mutagenesisi13P → S: No production of pili. 1 Publication1
Mutagenesisi58D → A: No production of propilin or pilin. 1 Publication1
Mutagenesisi68K → A: No production of propilin or pilin. 2 Publications1
Mutagenesisi68K → E: Resistant to phage R17 attachment. 2 Publications1
Mutagenesisi69A → E: No effect on propilin synthesis. No effect on pilus formation. Resistant to phage R17 attachment. 1 Publication1
Mutagenesisi71F → V: No effect on propilin synthesis. Defective pilus tip assembly. 1 Publication1
Mutagenesisi72G → D: No effect on propilin synthesis. No effect on pilus formation. 1 Publication1
Mutagenesisi73K → A or T: No effect on propilin synthesis. No effect on pilus formation. 2 Publications1
Mutagenesisi74D → G: No effect on propilin synthesis, no effect on pilus formation, resistant to phage R17 attachment (Ref.11). About 67% conjugation efficieny, E.coli still sensitive to CdiA-CT toxin (Ref.12). 2 Publications1
Mutagenesisi79K → A: No effect on propilin synthesis. Resistant to phage R17 attachment. 1 Publication1
Mutagenesisi79K → I: No effect on propilin synthesis. Defective pilus tip assembly. 1 Publication1
Mutagenesisi81V → I: Slightly reduced phage R17 attachment, reduced ability to retract. 1 Publication1
Mutagenesisi85E → A or G: No effect on propilin synthesis. Defective pilus tip assembly. 1 Publication1
Mutagenesisi93Y → D: Production of small amounts of propilin and pilin. 1 Publication1
Mutagenesisi97K → A, R or V: No effect on propilin synthesis. No effect on pilus formation. Inability to support R17 phage eclipse. 1 Publication1
Mutagenesisi97K → A: Reduced cleavage of propilin to pilin; when associated with A-100. 1 Publication1
Mutagenesisi98N → A: No effect on propilin synthesis. No effect on pilus formation. 1 Publication1
Mutagenesisi99V → A: No effect on propilin synthesis. No effect on pilus formation. Inability to support R17 phage eclipse. 1 Publication1
Mutagenesisi100K → A, R or T: No effect on propilin synthesis. No effect on pilus formation. Inability to support R17 phage eclipse. Reduced DNA transfer. 1 Publication1
Mutagenesisi100K → A: Reduced cleavage of propilin to pilin; when associated with A-97. 1 Publication1
Mutagenesisi101F → A: No effect on propilin synthesis. No effect on pilus formation. Inability to support R17 phage eclipse. Reduced DNA transfer. 1 Publication1
Mutagenesisi105F → V: No effect on propilin synthesis. No effect on pilus formation. Inability to support R17 phage eclipse. Reduced DNA transfer. 1 Publication1
Mutagenesisi111F → V: No effect on propilin synthesis. No effect on pilus formation. Inability to support R17 phage eclipse. Reduced DNA transfer. 1 Publication1
Mutagenesisi120G → C: Resistant to phage R17, conjugation normal, provides partial resistance to CdiA-CT toxin. 1 Publication1
Mutagenesisi120G → D: Resistant to phages R17 and QB attachment. 1 Publication1
Mutagenesisi121L → S: No effect on propilin synthesis. Defective pilus tip assembly. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000244871 – 51Leader peptide; cleaved by LepB1 PublicationAdd BLAST51
ChainiPRO_000002448852 – 121PilinAdd BLAST70

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP04737

PTM databases

iPTMnetiP04737

Interactioni

Subunit structurei

Monomer. Interacts with itself to form filaments; also interacts with TraQ.3 Publications

Protein-protein interaction databases

IntActiP04737, 1 interactor

Structurei

3D structure databases

ProteinModelPortaliP04737
SMRiP04737
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TraA family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OMAiSIVKWVV

Family and domain databases

InterProiView protein in InterPro
IPR008873 TraA
PfamiView protein in Pfam
PF05513 TraA, 1 hit
TIGRFAMsiTIGR02758 TraA_TIGR, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04737-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNAVLSVQGA SAPVKKKSFF SKFTRLNMLR LARAVIPAAV LMMFFPQLAM
60 70 80 90 100
AAGSSGQDLM ASGNTTVKAT FGKDSSVVKW VVLAEVLVGA VMYMMTKNVK
110 120
FLAGFAIISV FIAVGMAVVG L
Length:121
Mass (Da):12,768
Last modified:August 13, 1987 - v1
Checksum:iC65EEA3C6E7EF2A2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115G → V in AAA24910 (PubMed:6090426).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01147 Genomic DNA Translation: AAA24910.1
U01159 Genomic DNA Translation: AAC44177.1
M11322 Genomic DNA Translation: AAA98308.1
AP001918 Genomic DNA Translation: BAA97944.1
K03086 Genomic DNA Translation: AAA92543.1
K03087 Genomic DNA Translation: AAA92545.1
PIRiA23106 YQECFX
A29332 YQECF
RefSeqiNP_061453.1, NC_002483.1
NP_862919.1, NC_004998.1
WP_000994779.1, NZ_CP014273.1
YP_003937617.1, NC_014615.1
YP_009060156.1, NC_024956.1
YP_009068351.1, NC_025139.1
YP_009070616.1, NC_025175.1
YP_009071230.1, NC_025179.1

Genome annotation databases

GeneIDi1263548
1446483
20466906
20491481
20492684
20493302
9846166
PATRICifig|83333.107.peg.639

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01147 Genomic DNA Translation: AAA24910.1
U01159 Genomic DNA Translation: AAC44177.1
M11322 Genomic DNA Translation: AAA98308.1
AP001918 Genomic DNA Translation: BAA97944.1
K03086 Genomic DNA Translation: AAA92543.1
K03087 Genomic DNA Translation: AAA92545.1
PIRiA23106 YQECFX
A29332 YQECF
RefSeqiNP_061453.1, NC_002483.1
NP_862919.1, NC_004998.1
WP_000994779.1, NZ_CP014273.1
YP_003937617.1, NC_014615.1
YP_009060156.1, NC_024956.1
YP_009068351.1, NC_025139.1
YP_009070616.1, NC_025175.1
YP_009071230.1, NC_025179.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5LERelectron microscopy5.001A/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/2O57-121[»]
5LFBelectron microscopy5.001A/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/2O57-121[»]
ProteinModelPortaliP04737
SMRiP04737
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04737, 1 interactor

PTM databases

iPTMnetiP04737

Proteomic databases

PRIDEiP04737

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1263548
1446483
20466906
20491481
20492684
20493302
9846166
PATRICifig|83333.107.peg.639

Phylogenomic databases

OMAiSIVKWVV

Miscellaneous databases

PROiPR:P04737

Family and domain databases

InterProiView protein in InterPro
IPR008873 TraA
PfamiView protein in Pfam
PF05513 TraA, 1 hit
TIGRFAMsiTIGR02758 TraA_TIGR, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPIL1_ECOLI
AccessioniPrimary (citable) accession number: P04737
Secondary accession number(s): P14517
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 23, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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