DTPA_PECCP
ID DTPA_PECCP Reviewed; 506 AA.
AC C6DH09;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Dipeptide and tripeptide permease A {ECO:0000255|HAMAP-Rule:MF_01878};
GN Name=dtpA {ECO:0000255|HAMAP-Rule:MF_01878}; OrderedLocusNames=PC1_2017;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001657; ACT13058.1; -; Genomic_DNA.
DR RefSeq; WP_015840251.1; NC_012917.1.
DR AlphaFoldDB; C6DH09; -.
DR SMR; C6DH09; -.
DR EnsemblBacteria; ACT13058; ACT13058; PC1_2017.
DR KEGG; pct:PC1_2017; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_0_6; -.
DR OMA; QMMGVWF; -.
DR OrthoDB; 470322at2; -.
DR Proteomes; UP000002736; 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; 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; 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..506
FT /note="Dipeptide and tripeptide permease A"
FT /id="PRO_0000395179"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 58..61
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 83..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 134..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 177..180
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 202..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 244..248
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 270..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 298..322
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 344..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 376..385
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 407..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 438..461
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 483..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
SQ SEQUENCE 506 AA; 54864 MW; D056A699D8E9EC9A CRC64;
MSTANNNSES TESVSMNAFK QPKAFYLIFS IELWERFGYY GLQGIMAVYL VKMLGMSETD
SITLFSSFSA LVYGFVAIGG WLGDKVLGTK RVIVLGAIVL AIGYTMIAYS GHSVAWVYIG
MATIAVGNGL FKANPSALLS TCYAKDDPRL DGAFTMYYMA VNIGSFFSML ATPVLAANYG
WSVAFSLSVV GMILTLVNFM FCRKWVSTQG SQPDFQPINL KKLVITLAGI VVLVALSTWL
LHNQGVARWI LTIISLAVVA IFIKEMLAVS GAERRKMIVA LLLMLEAVVF FVLYNQMPTS
LNFFAIRNVE HSILGFAFEP EQYQALNPFW IMVASPLLAA VYNKMGDQLP MAHKFAIGMV
LCSGAFLVLP WGASMANEQG IVSVNWLILC YGLQSIGELM ISGLGLAMVA QLVPQRLMGF
IMGAWFLTSA GAAIIAGYVA NMMAVPENVV DPHVSLEVYS NVFMQIGIVT GIIAVLMMLT
APKLTRMTQD VATDVPADAA TTTASA
