DTPD_ECOLI
ID DTPD_ECOLI Reviewed; 493 AA.
AC P75742;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Dipeptide permease D;
GN Name=dtpD; Synonyms=ybgH; OrderedLocusNames=b0709, JW0699;
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=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(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 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).
CC -!- FUNCTION: Probable proton-dependent permease that transports
CC dipeptides. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpD
CC subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC73803.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35368.1; -; Genomic_DNA.
DR PIR; D64806; D64806.
DR RefSeq; NP_415237.1; NC_000913.3.
DR RefSeq; WP_001032689.1; NZ_SSZK01000033.1.
DR PDB; 4Q65; X-ray; 3.40 A; A=1-493.
DR PDBsum; 4Q65; -.
DR AlphaFoldDB; P75742; -.
DR SMR; P75742; -.
DR BioGRID; 4263335; 112.
DR BioGRID; 851691; 1.
DR DIP; DIP-11394N; -.
DR IntAct; P75742; 2.
DR STRING; 511145.b0709; -.
DR TCDB; 2.A.17.1.4; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; P75742; -.
DR PRIDE; P75742; -.
DR EnsemblBacteria; AAC73803; AAC73803; b0709.
DR EnsemblBacteria; BAA35368; BAA35368; BAA35368.
DR GeneID; 947368; -.
DR KEGG; ecj:JW0699; -.
DR KEGG; eco:b0709; -.
DR PATRIC; fig|1411691.4.peg.1564; -.
DR EchoBASE; EB3088; -.
DR eggNOG; COG3104; Bacteria.
DR InParanoid; P75742; -.
DR OMA; GMMMGLW; -.
DR PhylomeDB; P75742; -.
DR BioCyc; EcoCyc:B0709-MON; -.
DR BioCyc; MetaCyc:B0709-MON; -.
DR PRO; PR:P75742; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015333; F:peptide:proton symporter activity; IBA:GO_Central.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0035442; P:dipeptide transmembrane transport; IDA:EcoCyc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd17346; MFS_DtpA_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR HAMAP; MF_01880; PTR2_DtpD_subfam; 1.
DR InterPro; IPR023777; AA/pep_transptr_DtpD.
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..493
FT /note="Dipeptide permease D"
FT /id="PRO_0000064328"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..100
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..166
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..234
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..311
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..378
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..461
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 9..38
FT /evidence="ECO:0007829|PDB:4Q65"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 44..60
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 77..92
FT /evidence="ECO:0007829|PDB:4Q65"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 102..126
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 135..162
FT /evidence="ECO:0007829|PDB:4Q65"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:4Q65"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 212..232
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 234..254
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 267..297
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 314..331
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 342..369
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 379..393
FT /evidence="ECO:0007829|PDB:4Q65"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 411..437
FT /evidence="ECO:0007829|PDB:4Q65"
FT HELIX 452..480
FT /evidence="ECO:0007829|PDB:4Q65"
SQ SEQUENCE 493 AA; 54159 MW; 930DB6EDAE448B7D CRC64;
MNKHASQPRA IYYVVALQIW EYFSFYGMRA LLILYLTNQL KYNDTHAYEL FSAYCSLVYV
TPILGGFLAD KVLGNRMAVM LGALLMAIGH VVLGASEIHP SFLYLSLAII VCGYGLFKSN
VSCLLGELYE PTDPRRDGGF SLMYAAGNVG SIIAPIACGY AQEEYSWAMG FGLAAVGMIA
GLVIFLCGNR HFTHTRGVNK KVLRATNFLL PNWGWLLVLL VATPALITIL FWKEWSVYAL
IVATIIGLGV LAKIYRKAEN QKQRKELGLI VTLTFFSMLF WAFAQQGGSS ISLYIDRFVN
RDMFGYTVPT AMFQSINAFA VMLCGVFLAW VVKESVAGNR TVRIWGKFAL GLGLMSAGFC
ILTLSARWSA MYGHSSLPLM VLGLAVMGFA ELFIDPVAMS QITRIEIPGV TGVLTGIYML
LSGAIANYLA GVIADQTSQA SFDASGAINY SINAYIEVFD QITWGALACV GLVLMIWLYQ
ALKFRNRALA LES
