DTPC_ECOLI
ID DTPC_ECOLI Reviewed; 485 AA.
AC P39276; Q2M6H3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Dipeptide and tripeptide permease C {ECO:0000305};
DE AltName: Full=Dipeptide/tripeptide:H(+) symporter DtpC {ECO:0000305};
GN Name=dtpC {ECO:0000303|PubMed:19782088}; Synonyms=yjdL;
GN OrderedLocusNames=b4130, JW4091;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [5]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19703419; DOI=10.1016/j.bbrc.2009.08.098;
RA Ernst H.A., Pham A., Hald H., Kastrup J.S., Rahman M., Mirza O.;
RT "Ligand binding analyses of the putative peptide transporter YjdL from E.
RT coli display a significant selectivity towards dipeptides.";
RL Biochem. Biophys. Res. Commun. 389:112-116(2009).
RN [6]
RP GENE NAME.
RX PubMed=19782088; DOI=10.1016/j.jmb.2009.09.048;
RA Casagrande F., Harder D., Schenk A., Meury M., Ucurum Z., Engel A.,
RA Weitz D., Daniel H., Fotiadis D.;
RT "Projection structure of DtpD (YbgH), a prokaryotic member of the peptide
RT transporter family.";
RL J. Mol. Biol. 394:708-717(2009).
RN [7]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-388.
RX PubMed=22940668; DOI=10.1016/j.peptides.2012.08.012;
RA Jensen J.M., Simonsen F.C., Mastali A., Hald H., Lillebro I., Diness F.,
RA Olsen L., Mirza O.;
RT "Biophysical characterization of the proton-coupled oligopeptide
RT transporter YjdL.";
RL Peptides 38:89-93(2012).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-20 AND
RP GLU-388.
RX PubMed=21933132; DOI=10.2174/092986612799363109;
RA Jensen J.M., Ernst H., Wang X., Hald H., Ditta A.C., Ismat F., Rahman M.,
RA Mirza O.;
RT "Functional investigation of conserved membrane-embedded glutamate residues
RT in the proton-coupled peptide transporter YjdL.";
RL Protein Pept. Lett. 19:282-287(2012).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24440353; DOI=10.1016/j.febslet.2014.01.004;
RA Prabhala B.K., Aduri N.G., Jensen J.M., Ernst H.A., Iram N., Rahman M.,
RA Mirza O.;
RT "New insights into the substrate specificities of proton-coupled
RT oligopeptide transporters from E. coli by a pH sensitive assay.";
RL FEBS Lett. 588:560-565(2014).
CC -!- FUNCTION: Proton-dependent permease that transports di- and
CC tripeptides. Shows significantly higher specificity towards dipeptides
CC than tripeptides. Has a preference for dipeptides with a C-terminal Lys
CC residue. Can bind Ala-Lys, Lys-Ala, Ala-Ala. Can also transport alanine
CC and trialanine. {ECO:0000269|PubMed:19703419,
CC ECO:0000269|PubMed:21933132, ECO:0000269|PubMed:22940668,
CC ECO:0000269|PubMed:24440353}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for Ala-Lys {ECO:0000269|PubMed:24440353};
CC KM=0.51 mM for Lys-Ala {ECO:0000269|PubMed:24440353};
CC pH dependence:
CC Optimum pH is around 6.5. {ECO:0000269|PubMed:21933132};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22940668}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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DR EMBL; U14003; AAA97030.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77091.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78133.1; -; Genomic_DNA.
DR PIR; S56359; S56359.
DR RefSeq; NP_418554.1; NC_000913.3.
DR RefSeq; WP_000856829.1; NZ_SSZK01000018.1.
DR AlphaFoldDB; P39276; -.
DR SMR; P39276; -.
DR BioGRID; 4261129; 143.
DR STRING; 511145.b4130; -.
DR TCDB; 2.A.17.1.5; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; P39276; -.
DR PRIDE; P39276; -.
DR EnsemblBacteria; AAC77091; AAC77091; b4130.
DR EnsemblBacteria; BAE78133; BAE78133; BAE78133.
DR GeneID; 66671958; -.
DR GeneID; 948644; -.
DR KEGG; ecj:JW4091; -.
DR KEGG; eco:b4130; -.
DR PATRIC; fig|511145.12.peg.4262; -.
DR EchoBASE; EB2362; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_0_6; -.
DR InParanoid; P39276; -.
DR OMA; SFYGMRV; -.
DR PhylomeDB; P39276; -.
DR BioCyc; EcoCyc:YJDL-MON; -.
DR BioCyc; MetaCyc:YJDL-MON; -.
DR BRENDA; 7.4.2.5; 2026.
DR PRO; PR:P39276; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015333; F:peptide:proton symporter activity; IMP:EcoCyc.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0035442; P:dipeptide transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:EcoCyc.
DR GO; GO:0035443; P:tripeptide transmembrane transport; IMP:EcoCyc.
DR CDD; cd17346; MFS_DtpA_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR005279; Dipep/tripep_permease.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR00924; yjdL_sub1_fam; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..485
FT /note="Dipeptide and tripeptide permease C"
FT /id="PRO_0000064330"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..46
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..102
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..234
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..307
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..375
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..446
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT MUTAGEN 20
FT /note="E->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:21933132"
FT MUTAGEN 20
FT /note="E->D: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:21933132"
FT MUTAGEN 20
FT /note="E->Q: Decrease in activity. Abolishes the pH
FT dependency."
FT /evidence="ECO:0000269|PubMed:21933132"
FT MUTAGEN 388
FT /note="E->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:21933132"
FT MUTAGEN 388
FT /note="E->D: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:21933132"
FT MUTAGEN 388
FT /note="E->Q: Decrease in activity. Does not bind Ala-Lys
FT dipeptide."
FT /evidence="ECO:0000269|PubMed:21933132,
FT ECO:0000269|PubMed:22940668"
SQ SEQUENCE 485 AA; 53055 MW; ACBE0B947DE0CB61 CRC64;
MKTPSQPRAI YYIVAIQIWE YFSFYGMRAL LILYLTHQLG FDDNHAISLF SAYASLVYVT
PILGGWLADR LLGNRTAVIA GALLMTLGHV VLGIDTNSTF SLYLALAIII CGYGLFKSNI
SCLLGELYDE NDHRRDGGFS LLYAAGNIGS IAAPIACGLA AQWYGWHVGF ALAGGGMFIG
LLIFLSGHRH FQSTRSMDKK ALTSVKFALP VWSWLVVMLC LAPVFFTLLL ENDWSGYLLA
IVCLIAAQII ARMMIKFPEH RRALWQIVLL MFVGTLFWVL AQQGGSTISL FIDRFVNRQA
FNIEVPTALF QSVNAIAVML AGVVLAWLAS PESRGNSTLR VWLKFAFGLL LMACGFMLLA
FDARHAAADG QASMGVMISG LALMGFAELF IDPVAIAQIT RLKMSGVLTG IYMLATGAVA
NWLAGVVAQQ TTESQISGMA IAAYQRFFSQ MGEWTLACVA IIVVLAFATR FLFSTPTNMI
QESND
