DTPB_YERE8
ID DTPB_YERE8 Reviewed; 493 AA.
AC A1JRI8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Dipeptide and tripeptide permease B {ECO:0000255|HAMAP-Rule:MF_01879};
GN Name=dtpB {ECO:0000255|HAMAP-Rule:MF_01879}; OrderedLocusNames=YE2391;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL12443.1; -; Genomic_DNA.
DR RefSeq; WP_011816523.1; NC_008800.1.
DR RefSeq; YP_001006610.1; NC_008800.1.
DR AlphaFoldDB; A1JRI8; -.
DR SMR; A1JRI8; -.
DR EnsemblBacteria; CAL12443; CAL12443; YE2391.
DR KEGG; yen:YE2391; -.
DR PATRIC; fig|393305.7.peg.2545; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_0_6; -.
DR OMA; WNYGFVA; -.
DR Proteomes; UP000000642; 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..493
FT /note="Dipeptide and tripeptide permease B"
FT /id="PRO_0000395191"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 49..52
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 74..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 104..106
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 128..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 168..169
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 191..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 255..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 289..311
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 333..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 372..379
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 401..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 446..456
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 478..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
SQ SEQUENCE 493 AA; 54208 MW; 34139DEF67C92E8E CRC64;
MERSTPTGLL QQPKPFFMIF FVELWERFGY YGVQGILAVF FVQQLGFSQE QAFVTFGAFA
ALVYGLISIG GYVGDHLLGT KRTMVLGAVV LAAGYFATGL SLYQPNLIFF ALGTIAVGNG
LFKANPASLL SKCYPPKDPR LDGAFTLFYM SINIGSLLSL SLAPVIAERF GYTVTYYLCG
IGLIFALLVY FCCRHMVRHI GSEPDTKPLN WRNLLLVLLG SAVMICVCAW LMNHVFIANL
VLIALSLIVV FIFFREASKQ DRLGRNKMFV AFILMIEAIV FYVLYAQMPT SLNFFAINNV
HHEILGFSIN PVSFQALNPF WVVVASPILA SIYTRLGSQN RDLSMPAKFT LGMFLCSLGF
LTAAAAGMWF ADAQGLTSPW FIVLVYLFQS LGELMISALG LAMVAALVPQ YLMGFILGMW
FLTQAASFLI GGYVATFTAT PEGMTDPLET LPIYTDVFGK IGMVTLVIAL VMALLIPWLN
RMINSSAAED AVA
