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Pilin (F-pilin)

 PIL1_ECOLI              Reviewed;         121 AA.
P04737; P14517;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
23-MAY-2018, entry version 101.
RecName: Full=Pilin;
AltName: Full=F-pilin;
Flags: Precursor;
Name=traA; OrderedLocusNames=ECOK12F074;
Escherichia coli (strain K12).
Plasmid F, Plasmid IncFI R386, Plasmid IncFI ColV2-K94, and
Plasmid IncFI ColVBtrp.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 52-59,
ACETYLATION AT ALA-52, AND FUNCTION.
PLASMID=F;
PubMed=6090426;
Frost L.S., Paranchych W., Willetts N.S.;
"DNA sequence of the F traALE region that includes the gene for F
pilin.";
J. Bacteriol. 160:395-401(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=F;
PubMed=7915817;
Frost L.S., Ippen-Ihler K., Skurray R.A.;
"Analysis of the sequence and gene products of the transfer region of
the F sex factor.";
Microbiol. Rev. 58:162-210(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=IncFI ColV2-K94, IncFI ColVBtrp, and IncFI R386;
PubMed=2999074;
Frost L.S., Finlay B.B., Opgenorth A., Paranchych W., Lee J.S.;
"Characterization and sequence analysis of pilin from F-like
plasmids.";
J. Bacteriol. 164:1238-1247(1985).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / CR63; PLASMID=F;
Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
"Complete nucleotide sequence of the F plasmid: its implications for
organization and diversification of plasmid genomes.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[5]
BACTERIOPHAGE ATTACHMENT TO PILIN, AND MUTAGENESIS OF GLY-9; PRO-13;
LYS-68; LYS-73; VAL-81 AND GLY-120.
PubMed=2906110; DOI=10.1007/BF00333409;
Frost L.S., Paranchych W.;
"DNA sequence analysis of point mutations in traA, the F pilin gene,
reveal two domains involved in F-specific bacteriophage attachment.";
Mol. Gen. Genet. 213:134-139(1988).
[6]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TOPOLOGY.
PLASMID=F;
PubMed=1464628;
Paiva W.D., Grossman T., Silverman P.M.;
"Characterization of F-pilin as an inner membrane component of
Escherichia coli K12.";
J. Biol. Chem. 267:26191-26197(1992).
[7]
INTERACTION WITH TRAQ.
PLASMID=F;
PubMed=8095257; DOI=10.1128/jb.175.5.1384-1391.1993;
Maneewannakul K., Maneewannakul S., Ippen-Ihler K.;
"Synthesis of F pilin.";
J. Bacteriol. 175:1384-1391(1993).
[8]
CLEAVAGE OF LEADER PEPTIDE BY LEPB.
PLASMID=F;
PubMed=8682775;
Majdalani N., Ippen-Ihler K.;
"Membrane insertion of the F-pilin subunit is Sec independent but
requires leader peptidase B and the proton motive force.";
J. Bacteriol. 178:3742-3747(1996).
[9]
MUTAGENESIS OF LEU-121.
PubMed=9641980; DOI=10.1006/jmbi.1998.1773;
Rondot S., Anthony K.G., Duebel S., Ida N., Wiemann S., Beyreuther K.,
Frost L.S., Little M., Breitling F.;
"Epitopes fused to F-pilin are incorporated into functional
recombinant pili.";
J. Mol. Biol. 279:589-603(1998).
[10]
INTERACTION WITH TRAQ.
PLASMID=F;
PubMed=10564517; DOI=10.1046/j.1365-2958.1999.01640.x;
Harris R.L., Sholl K.A., Conrad M.N., Dresser M.E., Silverman P.M.;
"Interaction between the F plasmid TraA (F-pilin) and TraQ proteins.";
Mol. Microbiol. 34:780-791(1999).
[11]
MUTAGENESIS OF ASP-58; LYS-68; ALA-69; PHE-71; GLY-72; LYS-73; ASP-74;
LYS-79; GLU-85; TYR-93; LYS-97; ASN-98; VAL-99; LYS-100; PHE-101;
PHE-105 AND PHE-111.
PLASMID=F;
PubMed=11849547; DOI=10.1046/j.1365-2958.2002.02731.x;
Manchak J., Anthony K.G., Frost L.S.;
"Mutational analysis of F-pilin reveals domains for pilus assembly,
phage infection and DNA transfer.";
Mol. Microbiol. 43:195-205(2002).
[12]
FUNCTION AS RECEPTOR FOR CDIA-CT, DISRUPTION PHENOTYPE, AND
MUTAGENESIS OF ASP-74 AND GLY-120.
STRAIN=K12 / X90; PLASMID=F;
PubMed=24889811; DOI=10.1111/mmi.12658;
Beck C.M., Diner E.J., Kim J.J., Low D.A., Hayes C.S.;
"The F pilus mediates a novel pathway of CDI toxin import.";
Mol. Microbiol. 93:276-290(2014).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:1464628, ECO:0000269|PubMed:24889811,
ECO:0000269|PubMed:6090426}.
-!- SUBUNIT: Monomer. Interacts with itself to form filaments; also
interacts with TraQ. {ECO:0000269|PubMed:10564517,
ECO:0000269|PubMed:1464628, ECO:0000269|PubMed:8095257}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:1464628}; Multi-pass membrane protein
{ECO:0000269|PubMed:1464628}. Secreted
{ECO:0000269|PubMed:1464628}. Note=Propilin is directed to the
inner membrane, where it is cleaved and acetylated. Mature pilin
forms filaments that are secreted to form the conjugative pilus.
-!- DISRUPTION PHENOTYPE: Loss of sensitivity to toxin CdiA-CT.
{ECO:0000269|PubMed:24889811}.
-!- SIMILARITY: Belongs to the TraA family. {ECO:0000305}.
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EMBL; K01147; AAA24910.1; -; Genomic_DNA.
EMBL; U01159; AAC44177.1; -; Genomic_DNA.
EMBL; M11322; AAA98308.1; -; Genomic_DNA.
EMBL; AP001918; BAA97944.1; -; Genomic_DNA.
EMBL; K03086; AAA92543.1; -; Genomic_DNA.
EMBL; K03087; AAA92545.1; -; Genomic_DNA.
PIR; A23106; YQECFX.
PIR; A29332; YQECF.
RefSeq; NP_061453.1; NC_002483.1.
RefSeq; NP_862919.1; NC_004998.1.
RefSeq; WP_000994779.1; NZ_CP014273.1.
RefSeq; YP_003937617.1; NC_014615.1.
RefSeq; YP_009060156.1; NC_024956.1.
RefSeq; YP_009068351.1; NC_025139.1.
RefSeq; YP_009070616.1; NC_025175.1.
RefSeq; YP_009071230.1; NC_025179.1.
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.
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.
PDBsum; 5LER; -.
PDBsum; 5LFB; -.
ProteinModelPortal; P04737; -.
SMR; P04737; -.
IntAct; P04737; 1.
iPTMnet; P04737; -.
PRIDE; P04737; -.
GeneID; 1263548; -.
GeneID; 1446483; -.
GeneID; 20466906; -.
GeneID; 20491481; -.
GeneID; 20492684; -.
GeneID; 20493302; -.
GeneID; 9846166; -.
PATRIC; fig|83333.107.peg.639; -.
OMA; SIVKWVV; -.
PRO; PR:P04737; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000746; P:conjugation; IEA:UniProtKB-KW.
InterPro; IPR008873; TraA.
Pfam; PF05513; TraA; 1.
TIGRFAMs; TIGR02758; TraA_TIGR; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell inner membrane; Cell membrane;
Conjugation; Direct protein sequencing; Membrane; Plasmid; Secreted;
Transmembrane; Transmembrane helix.
PROPEP 1 51 Leader peptide; cleaved by LepB.
{ECO:0000269|PubMed:6090426}.
/FTId=PRO_0000024487.
CHAIN 52 121 Pilin.
/FTId=PRO_0000024488.
TOPO_DOM 1 75 Periplasmic.
{ECO:0000269|PubMed:1464628}.
TRANSMEM 76 96 Helical.
TOPO_DOM 97 100 Cytoplasmic.
{ECO:0000269|PubMed:1464628}.
TRANSMEM 101 121 Helical.
MOD_RES 52 52 N-acetylalanine.
{ECO:0000269|PubMed:6090426}.
MUTAGEN 9 9 G->S: No production of pili.
{ECO:0000269|PubMed:2906110}.
MUTAGEN 13 13 P->S: No production of pili.
{ECO:0000269|PubMed:2906110}.
MUTAGEN 58 58 D->A: No production of propilin or pilin.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 68 68 K->A: No production of propilin or pilin.
{ECO:0000269|PubMed:11849547,
ECO:0000269|PubMed:2906110}.
MUTAGEN 68 68 K->E: Resistant to phage R17 attachment.
{ECO:0000269|PubMed:11849547,
ECO:0000269|PubMed:2906110}.
MUTAGEN 69 69 A->E: No effect on propilin synthesis. No
effect on pilus formation. Resistant to
phage R17 attachment.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 71 71 F->V: No effect on propilin synthesis.
Defective pilus tip assembly.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 72 72 G->D: No effect on propilin synthesis. No
effect on pilus formation.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 73 73 K->A,T: No effect on propilin synthesis.
No effect on pilus formation.
{ECO:0000269|PubMed:11849547,
ECO:0000269|PubMed:2906110}.
MUTAGEN 74 74 D->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).
{ECO:0000269|PubMed:11849547,
ECO:0000269|PubMed:24889811}.
MUTAGEN 79 79 K->A: No effect on propilin synthesis.
Resistant to phage R17 attachment.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 79 79 K->I: No effect on propilin synthesis.
Defective pilus tip assembly.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 81 81 V->I: Slightly reduced phage R17
attachment, reduced ability to retract.
{ECO:0000269|PubMed:2906110}.
MUTAGEN 85 85 E->A,G: No effect on propilin synthesis.
Defective pilus tip assembly.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 93 93 Y->D: Production of small amounts of
propilin and pilin.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 97 97 K->A,R,V: No effect on propilin
synthesis. No effect on pilus formation.
Inability to support R17 phage eclipse.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 97 97 K->A: Reduced cleavage of propilin to
pilin; when associated with A-100.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 98 98 N->A: No effect on propilin synthesis. No
effect on pilus formation.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 99 99 V->A: No effect on propilin synthesis. No
effect on pilus formation. Inability to
support R17 phage eclipse.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 100 100 K->A,R,T: No effect on propilin
synthesis. No effect on pilus formation.
Inability to support R17 phage eclipse.
Reduced DNA transfer.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 100 100 K->A: Reduced cleavage of propilin to
pilin; when associated with A-97.
{ECO:0000269|PubMed:11849547}.
MUTAGEN 101 101 F->A: No effect on propilin synthesis. No
effect on pilus formation. Inability to
support R17 phage eclipse. Reduced DNA
transfer. {ECO:0000269|PubMed:11849547}.
MUTAGEN 105 105 F->V: No effect on propilin synthesis. No
effect on pilus formation. Inability to
support R17 phage eclipse. Reduced DNA
transfer. {ECO:0000269|PubMed:11849547}.
MUTAGEN 111 111 F->V: No effect on propilin synthesis. No
effect on pilus formation. Inability to
support R17 phage eclipse. Reduced DNA
transfer. {ECO:0000269|PubMed:11849547}.
MUTAGEN 120 120 G->C: Resistant to phage R17, conjugation
normal, provides partial resistance to
CdiA-CT toxin.
{ECO:0000269|PubMed:24889811}.
MUTAGEN 120 120 G->D: Resistant to phages R17 and QB
attachment. {ECO:0000269|PubMed:2906110}.
MUTAGEN 121 121 L->S: No effect on propilin synthesis.
Defective pilus tip assembly.
{ECO:0000269|PubMed:9641980}.
CONFLICT 115 115 G -> V (in Ref. 1; AAA24910).
{ECO:0000305}.
SEQUENCE 121 AA; 12768 MW; C65EEA3C6E7EF2A2 CRC64;
MNAVLSVQGA SAPVKKKSFF SKFTRLNMLR LARAVIPAAV LMMFFPQLAM AAGSSGQDLM
ASGNTTVKAT FGKDSSVVKW VVLAEVLVGA VMYMMTKNVK FLAGFAIISV FIAVGMAVVG
L


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