DTPD_ECO57
ID DTPD_ECO57 Reviewed; 493 AA.
AC Q8X9D3; Q7AGL2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Dipeptide permease D;
GN Name=dtpD; OrderedLocusNames=Z0860, ECs0734;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=O157:H7 / EHEC;
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).
CC -!- FUNCTION: Probable proton-dependent permease that transports
CC dipeptides. {ECO:0000269|PubMed:19782088}.
CC -!- SUBUNIT: Monomer in solution. Exhibits a doughnut-like shape with a
CC central, shallow depression and has a diameter of 8 nm.
CC {ECO:0000269|PubMed:19782088}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:19782088}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19782088}.
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; AE005174; AAG55032.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34157.1; -; Genomic_DNA.
DR PIR; D85571; D85571.
DR PIR; F90720; F90720.
DR RefSeq; NP_308761.1; NC_002695.1.
DR RefSeq; WP_001032707.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X9D3; -.
DR SMR; Q8X9D3; -.
DR STRING; 155864.EDL933_0775; -.
DR EnsemblBacteria; AAG55032; AAG55032; Z0860.
DR EnsemblBacteria; BAB34157; BAB34157; ECs_0734.
DR GeneID; 917103; -.
DR KEGG; ece:Z0860; -.
DR KEGG; ecs:ECs_0734; -.
DR PATRIC; fig|386585.9.peg.850; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_0_6; -.
DR OMA; GMMMGLW; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015333; F:peptide:proton symporter activity; IEA:UniProtKB-UniRule.
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 Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..493
FT /note="Dipeptide permease D"
FT /id="PRO_0000395295"
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..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..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"
SQ SEQUENCE 493 AA; 54230 MW; 7FF2F29DBD3C4B61 CRC64;
MNKHASQPRA IYYVVALQIW EYFSFYGMRA LLILYLTNQL KYNDTHAYEL FSAYCSLVYV
TPILGGFLAD KVLGNRMAVM LGALLMAIGH VVLGASEIHP SFLYLSLAII VCGYGLFKSN
VSCLLGELYE PTDPRRDGGF SLMYAAGNVG SIIAPIACGY AQEEYSWAMG FGLAAVGMIA
GLVIFLCGNR HFTHTRGVNK KVLRATNFLL PNWGWLLVLL VATPALITVL FWKEWSVYAL
IVATIIGLGV LAKIYRKAEN QKQRKELRLI VTLTFFSMLF WAFAQQGGSS ISLYIDRFVN
RDMFGYTVPT AMFQSINAFA VMLCGVFLAW VVKESVAGNR TVRIWGKFAL GLGLMSAGFC
ILTLSARWSA MYGHSSLPLM VLGLAVMGFA ELFIDPVAMS QITRIEIPGV TGVLTGIYML
LSGAIANYLA GVIADQTSQA SFDASGAINY SINAYIEVFD QITWGALACV GVVLMIWLYQ
ALKFRNRALA LES
