DTPA_ECOL6
ID DTPA_ECOL6 Reviewed; 500 AA.
AC Q8FH91;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Dipeptide and tripeptide permease A {ECO:0000255|HAMAP-Rule:MF_01878};
GN Name=dtpA {ECO:0000255|HAMAP-Rule:MF_01878}; Synonyms=tppB;
GN OrderedLocusNames=c2026;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Proton-dependent permease that transports di- and
CC tripeptides. {ECO:0000255|HAMAP-Rule:MF_01878}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01878}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01878}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01878}.
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DR EMBL; AE014075; AAN80486.1; -; Genomic_DNA.
DR RefSeq; WP_000100937.1; NC_004431.1.
DR AlphaFoldDB; Q8FH91; -.
DR SMR; Q8FH91; -.
DR STRING; 199310.c2026; -.
DR EnsemblBacteria; AAN80486; AAN80486; c2026.
DR KEGG; ecc:c2026; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_0_6; -.
DR OMA; QMMGVWF; -.
DR BioCyc; ECOL199310:C2026-MON; -.
DR Proteomes; UP000001410; 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_01878; PTR2_DtpA_subfam; 1.
DR InterPro; IPR023517; AA/pep_transptr_DtpA.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..500
FT /note="Dipeptide and tripeptide permease A"
FT /id="PRO_0000064324"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 22..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 45..59
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 81..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 111
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 133..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 175..178
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 200..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 241..246
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 268..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 296..320
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 342..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 374..378
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 400..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 436..459
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 481..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
SQ SEQUENCE 500 AA; 54039 MW; EDBB67C4EC247F5C CRC64;
MSTANQKPTE SVSLNAFKQP KAFYLIFSIE LWERFGYYGL QGIMAVYLVK QLGMSEADSI
TLFSSFSALV YGLVAIGGWL GDKVLGTKRV IMLGAIVLAI GYALVAWSGH DAGIVYMGMA
AIAVGNGLFK ANPSSLLSTC YEKNDPRLDG AFTMYYMSVN IGSFFSMIAT PWLAAKYGWS
VAFALSVVGL LITIVNFAFC QRWVKQYGSK PDFEPINYRN LLLTIIGVVA LIAIATWLLH
NQEVARMALG VVAFGIVVIF GKEAFAMKGA ARRKMIVAFI LMLEAIIFFV LYSQMPTSLN
FFAIRNVEHT ILGLAVEPEQ YQALNPFWII IGSPILAAIY NKMGDTLPMP TKFAIGMVMC
SGAFLILPLG AKFASDAGIV SVSWLVASYG LQSIGELMIS GLGLAMVAQL VPQRLMGFIM
GSWFLTTAGA NLIGGYVAGM MAVPDNVTDP LMSLEVYGRV FLQIGVATAV IAVLMLFTAP
KLHRMTQDDA ADKAAKAAVA
