DTPB_ECOLI
ID DTPB_ECOLI Reviewed; 489 AA.
AC P36837; P76706; Q2M7F8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Dipeptide and tripeptide permease B;
GN Name=dtpB; Synonyms=yhiP; OrderedLocusNames=b3496, JW3463;
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=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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, AND ACTIVITY REGULATION.
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
CC tripeptides. Has a clear preference for dipeptides and tripeptides
CC composed of L-amino acids, and discriminates dipeptides on the basis of
CC the position of charges within the substrate.
CC {ECO:0000269|PubMed:18485005}.
CC -!- ACTIVITY REGULATION: Inhibited by CCCP but unaffected by sodium
CC depletion. {ECO:0000269|PubMed:18485005}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Although DtpB appears to represent a system of lower
CC affinity, there is an obvious redundancy in substrate specificity as
CC compared with DtpA.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpB
CC subfamily. {ECO:0000305}.
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DR EMBL; U00039; AAB18472.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76521.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77798.1; -; Genomic_DNA.
DR PIR; C65147; C65147.
DR RefSeq; NP_417953.1; NC_000913.3.
DR RefSeq; WP_001098652.1; NZ_SSZK01000042.1.
DR AlphaFoldDB; P36837; -.
DR SMR; P36837; -.
DR BioGRID; 4261541; 185.
DR DIP; DIP-12369N; -.
DR IntAct; P36837; 1.
DR STRING; 511145.b3496; -.
DR TCDB; 2.A.17.1.3; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; P36837; -.
DR PRIDE; P36837; -.
DR EnsemblBacteria; AAC76521; AAC76521; b3496.
DR EnsemblBacteria; BAE77798; BAE77798; BAE77798.
DR GeneID; 948006; -.
DR KEGG; ecj:JW3463; -.
DR KEGG; eco:b3496; -.
DR PATRIC; fig|511145.12.peg.3598; -.
DR EchoBASE; EB2144; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_0_6; -.
DR InParanoid; P36837; -.
DR OMA; WNYGFVA; -.
DR PhylomeDB; P36837; -.
DR BioCyc; EcoCyc:YHIP-MON; -.
DR BioCyc; MetaCyc:YHIP-MON; -.
DR PRO; PR:P36837; -.
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; IDA: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_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; 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..489
FT /note="Dipeptide and tripeptide permease B"
FT /id="PRO_0000064329"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..52
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..106
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..172
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..233
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..311
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..380
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..456
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 489 AA; 53575 MW; 80AB5CE4E3880448 CRC64;
MNTTTPMGML QQPRPFFMIF FVELWERFGY YGVQGVLAVF FVKQLGFSQE QAFVTFGAFA
ALVYGLISIG GYVGDHLLGT KRTIVLGALV LAIGYFMTGM SLLKPDLIFI ALGTIAVGNG
LFKANPASLL SKCYPPKDPR LDGAFTLFYM SINIGSLIAL SLAPVIADRF GYSVTYNLCG
AGLIIALLVY IACRGMVKDI GSEPDFRPMS FSKLLYVLLG SVVMIFVCAW LMHNVEVANL
VLIVLSIVVT IIFFRQAFKL DKTGRNKMFV AFVLMLEAVV FYILYAQMPT SLNFFAINNV
HHEILGFSIN PVSFQALNPF WVVLASPILA GIYTHLGNKG KDLSMPMKFT LGMFMCSLGF
LTAAAAGMWF ADAQGLTSPW FIVLVYLFQS LGELFISALG LAMIAALVPQ HLMGFILGMW
FLTQAAAFLL GGYVATFTAV PDNITDPLET LPVYTNVFGK IGLVTLGVAV VMLLMVPWLK
RMIATPESH
