ID   DTPB_EDWTE              Reviewed;         491 AA.
AC   D0ZGL2;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Dipeptide and tripeptide permease B {ECO:0000255|HAMAP-Rule:MF_01879};
GN   Name=dtpB {ECO:0000255|HAMAP-Rule:MF_01879}; OrderedLocusNames=ETAE_3352;
OS   Edwardsiella tarda (strain EIB202).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=498217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EIB202;
RX   PubMed=19865481; DOI=10.1371/journal.pone.0007646;
RA   Wang Q., Yang M., Xiao J., Wu H., Wang X., Lv Y., Xu L., Zheng H., Wang S.,
RA   Zhao G., Liu Q., Zhang Y.;
RT   "Genome sequence of the versatile fish pathogen Edwardsiella tarda provides
RT   insights into its adaptation to broad host ranges and intracellular
RT   niches.";
RL   PLoS ONE 4:E7646-E7646(2009).
CC   -!- FUNCTION: Proton-dependent permease that transports di- and
CC       tripeptides. {ECO:0000255|HAMAP-Rule:MF_01879}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01879}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01879}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC       dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01879}.
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DR   EMBL; CP001135; ACY86183.1; -; Genomic_DNA.
DR   RefSeq; WP_012850149.1; NC_013508.1.
DR   AlphaFoldDB; D0ZGL2; -.
DR   SMR; D0ZGL2; -.
DR   EnsemblBacteria; ACY86183; ACY86183; ETAE_3352.
DR   GeneID; 58257214; -.
DR   KEGG; etr:ETAE_3352; -.
DR   HOGENOM; CLU_004790_0_0_6; -.
DR   OMA; WNYGFVA; -.
DR   OrthoDB; 470322at2; -.
DR   Proteomes; UP000002634; 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:0042937; F:tripeptide transmembrane transporter 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_01879; PTR2_DtpB_subfam; 1.
DR   InterPro; IPR023778; AA/pep_transptr_DtpB.
DR   InterPro; IPR005279; Dipep/tripep_permease.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR000109; POT_fam.
DR   InterPro; IPR018456; PTR2_symporter_CS.
DR   PANTHER; PTHR11654; PTHR11654; 1.
DR   PANTHER; PTHR11654:SF102; PTHR11654:SF102; 1.
DR   Pfam; PF00854; PTR2; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00924; yjdL_sub1_fam; 1.
DR   PROSITE; PS01023; PTR2_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..491
FT                   /note="Dipeptide and tripeptide permease B"
FT                   /id="PRO_0000395184"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        48..51
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        73..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        103..105
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        127..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        167..171
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        193..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        232
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        254..266
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        288..312
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        313..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        336..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        371..378
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        400..423
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        445..454
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT   TOPO_DOM        476..491
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
SQ   SEQUENCE   491 AA;  53531 MW;  565F9094D78B53A0 CRC64;
     MNNTAPGLLH QPKPFFMIFF VELWERFGYY GVQGILAVFF VKQLGFSQEQ AFITFGAFAA
     LVYGLISIGG YVGDHLLGTK RTMVLGAIVL ALGYFMTGMS LLKPEMIFIA LGTIAVGNGL
     FKANPASLLS KCYPPKDPRL DGAFTLFYMS INIGSLLSLS LAPIIAERFG YAVTYNLCGL
     GLIIALLVYF ACRGMVRSIG SAPDHQPLNY GKLLLVLAGA VVMIFLCAWL MHNVGVANIV
     LIAVSAVVLY FFFREAFKQD KTGRNRMFVA FILMIEAVLF YILYAQMPTS LNFFAINNVR
     HELLGFAINP VSFQALNPFW VVVASPILAS IYTRLGSRGR DMTMPTKFTL GMLLCSLGFL
     TAAAAGMWFA DAQGLTSPWF VVLVYLFQSL GELMISALGL AMVAALVPQY LMGFILGMWF
     LTQAAAFLLG GYVATFTAVP AGIHDPLQTL PIYTGVFGKI GIATLIVTLV MAAMVPWLNR
     MMNTPADGQK A