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2.A.17.1.5
Peptide transporter, YjdL (preference for di-peptides) (Ernst et al., 2009; Gabrielsen et al., 2011; Jensen et al., 2011).  The motif, ExxERFxxYY has been shown to be involved in proton translocation, and the nearby K117 may play a dual role in protonation and substrate binding (Jensen et al. 2014).

Accession Number:P39276
Protein Name:Probable dipeptide and tripeptide permease YjdL
Length:485
Molecular Weight:53055.00
Species:Escherichia coli (strain K12) [83333]
Number of TMSs:14
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate peptides

Cross database links:

Genevestigator: P39276
EchoBASE: EB2362
EcoGene: EG12469
eggNOG: COG3104
HEGENOM: HBG586603
Entrez Gene ID: 948644   
Pfam: PF00854   
KEGG: ecj:JW4091    eco:b4130   

Gene Ontology

GO:0005887 C:integral to plasma membrane
GO:0015333 F:peptide:hydrogen symporter activity
GO:0042938 P:dipeptide transport
GO:0015031 P:protein transport

References (5)

[1] “Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.”  Burland V.D.et.al.   7610040
[2] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[3] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[4] “Global topology analysis of the Escherichia coli inner membrane proteome.”  Daley D.O.et.al.   15919996
[5] “Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides.”  Ernst H.A.et.al.   19703419

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKTPSQPRAI YYIVAIQIWE YFSFYGMRAL LILYLTHQLG FDDNHAISLF SAYASLVYVT 
61:	PILGGWLADR LLGNRTAVIA GALLMTLGHV VLGIDTNSTF SLYLALAIII CGYGLFKSNI 
121:	SCLLGELYDE NDHRRDGGFS LLYAAGNIGS IAAPIACGLA AQWYGWHVGF ALAGGGMFIG 
181:	LLIFLSGHRH FQSTRSMDKK ALTSVKFALP VWSWLVVMLC LAPVFFTLLL ENDWSGYLLA 
241:	IVCLIAAQII ARMMIKFPEH RRALWQIVLL MFVGTLFWVL AQQGGSTISL FIDRFVNRQA 
301:	FNIEVPTALF QSVNAIAVML AGVVLAWLAS PESRGNSTLR VWLKFAFGLL LMACGFMLLA 
361:	FDARHAAADG QASMGVMISG LALMGFAELF IDPVAIAQIT RLKMSGVLTG IYMLATGAVA 
421:	NWLAGVVAQQ TTESQISGMA IAAYQRFFSQ MGEWTLACVA IIVVLAFATR FLFSTPTNMI 
481:	QESND