DTPA_ECOLI
ID DTPA_ECOLI Reviewed; 500 AA.
AC P77304;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dipeptide and tripeptide permease A;
GN Name=dtpA; Synonyms=tppB, ydgR; OrderedLocusNames=b1634, JW1626;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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 FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=15175316; DOI=10.1128/jb.186.12.4019-4024.2004;
RA Goh E.B., Siino D.F., Igo M.M.;
RT "The Escherichia coli tppB (ydgR) gene represents a new class of OmpR-
RT regulated genes.";
RL J. Bacteriol. 186:4019-4024(2004).
RN [5]
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 [6]
RP FUNCTION IN PEPTIDE TRANSPORT, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17158458; DOI=10.1074/jbc.m604866200;
RA Weitz D., Harder D., Casagrande F., Fotiadis D., Obrdlik P., Kelety B.,
RA Daniel H.;
RT "Functional and structural characterization of a prokaryotic peptide
RT transporter with features similar to mammalian PEPT1.";
RL J. Biol. Chem. 282:2832-2839(2007).
RN [7]
RP FUNCTION.
RX PubMed=18485005; DOI=10.1111/j.1742-4658.2008.06477.x;
RA Harder D., Stolz J., Casagrande F., Obrdlik P., Weitz D., Fotiadis D.,
RA Daniel H.;
RT "DtpB (YhiP) and DtpA (TppB, YdgR) are prototypical proton-dependent
RT peptide transporters of Escherichia coli.";
RL FEBS J. 275:3290-3298(2008).
CC -!- FUNCTION: Proton-dependent permease that transports di- and tripeptides
CC as well as structurally related peptidomimetics such as
CC aminocephalosporins into the cell. Has a clear preference for
CC dipeptides and tripeptides composed of L-amino acids, and discriminates
CC dipeptides on the basis of the position of charges within the
CC substrate. {ECO:0000269|PubMed:15175316, ECO:0000269|PubMed:17158458,
CC ECO:0000269|PubMed:18485005}.
CC -!- SUBUNIT: Monomer (Probable). Has a crown-like structure with a diameter
CC of 8 nm and a central density. {ECO:0000269|PubMed:17158458,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Transcriptionally activated by the EnvZ/OmpR regulatory
CC system. {ECO:0000269|PubMed:15175316}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpA
CC subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74706.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15395.1; -; Genomic_DNA.
DR PIR; D64920; D64920.
DR RefSeq; NP_416151.1; NC_000913.3.
DR RefSeq; WP_000100932.1; NZ_STEB01000003.1.
DR PDB; 6GS1; X-ray; 3.29 A; A=2-500.
DR PDB; 6GS4; X-ray; 2.65 A; A=2-500.
DR PDB; 6GS7; X-ray; 3.30 A; A=2-500.
DR PDBsum; 6GS1; -.
DR PDBsum; 6GS4; -.
DR PDBsum; 6GS7; -.
DR AlphaFoldDB; P77304; -.
DR SASBDB; P77304; -.
DR SMR; P77304; -.
DR BioGRID; 4260260; 253.
DR STRING; 511145.b1634; -.
DR TCDB; 2.A.17.1.2; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR jPOST; P77304; -.
DR PaxDb; P77304; -.
DR PRIDE; P77304; -.
DR ABCD; P77304; 5 sequenced antibodies.
DR EnsemblBacteria; AAC74706; AAC74706; b1634.
DR EnsemblBacteria; BAA15395; BAA15395; BAA15395.
DR GeneID; 58463902; -.
DR GeneID; 947436; -.
DR KEGG; ecj:JW1626; -.
DR KEGG; eco:b1634; -.
DR PATRIC; fig|1411691.4.peg.626; -.
DR EchoBASE; EB3698; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_0_6; -.
DR InParanoid; P77304; -.
DR OMA; QMMGVWF; -.
DR PhylomeDB; P77304; -.
DR BioCyc; EcoCyc:B1634-MON; -.
DR BioCyc; MetaCyc:B1634-MON; -.
DR BRENDA; 7.4.2.5; 2026.
DR PRO; PR:P77304; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015333; F:peptide:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0035442; P:dipeptide transmembrane transport; IDA: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 HAMAP; MF_01878; PTR2_DtpA_subfam; 1.
DR InterPro; IPR023517; AA/pep_transptr_DtpA.
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; 1.
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 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Peptide transport; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..500
FT /note="Dipeptide and tripeptide permease A"
FT /id="PRO_0000064323"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..59
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..178
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..246
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..320
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..378
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..459
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 21..50
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 56..72
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 87..106
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 147..176
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 179..199
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 218..240
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 242..266
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 269..292
FT /evidence="ECO:0007829|PDB:6GS4"
FT TURN 293..297
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:6GS4"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 324..340
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 349..372
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 382..398
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 416..439
FT /evidence="ECO:0007829|PDB:6GS4"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:6GS4"
FT HELIX 450..485
FT /evidence="ECO:0007829|PDB:6GS4"
SQ SEQUENCE 500 AA; 53991 MW; BFDCBE0BFC206C46 CRC64;
MSTANQKPTE SVSLNAFKQP KAFYLIFSIE LWERFGYYGL QGIMAVYLVK QLGMSEADSI
TLFSSFSALV YGLVAIGGWL GDKVLGTKRV IMLGAIVLAI GYALVAWSGH DAGIVYMGMA
AIAVGNGLFK ANPSSLLSTC YEKNDPRLDG AFTMYYMSVN IGSFFSMIAT PWLAAKYGWS
VAFALSVVGL LITIVNFAFC QRWVKQYGSK PDFEPINYRN LLLTIIGVVA LIAIATWLLH
NQEVARMALG VVAFGIVVIF GKEAFAMKGA ARRKMIVAFI LMLEAIIFFV LYSQMPTSLN
FFAIRNVEHS ILGLAVEPEQ YQALNPFWII IGSPILAAIY NKMGDTLPMP TKFAIGMVMC
SGAFLILPLG AKFASDAGIV SVSWLVASYG LQSIGELMIS GLGLAMVAQL VPQRLMGFIM
GSWFLTTAGA NLIGGYVAGM MAVPDNVTDP LMSLEVYGRV FLQIGVATAV IAVLMLLTAP
KLHRMTQDDA ADKAAKAAVA
