DTPT_LACLA
ID DTPT_LACLA Reviewed; 497 AA.
AC P0C2U2; P36574; Q9CHM6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Di-/tripeptide transporter;
GN Name=dtpT; OrderedLocusNames=LL0702; ORFNames=L104437;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Proton-dependent uptake of di- or tri-peptides.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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; AE005176; AAK04800.1; -; Genomic_DNA.
DR PIR; F86712; F86712.
DR RefSeq; NP_266858.1; NC_002662.1.
DR RefSeq; WP_010905519.1; NC_002662.1.
DR AlphaFoldDB; P0C2U2; -.
DR SMR; P0C2U2; -.
DR STRING; 272623.L104437; -.
DR TCDB; 2.A.17.1.1; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; P0C2U2; -.
DR EnsemblBacteria; AAK04800; AAK04800; L104437.
DR KEGG; lla:L104437; -.
DR PATRIC; fig|272623.7.peg.753; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_1_9; -.
DR OMA; QMMGVWF; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006857; P:oligopeptide transport; IEA:InterPro.
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 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; 2.
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 membrane; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..497
FT /note="Di-/tripeptide transporter"
FT /id="PRO_0000064322"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 56..64
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..83
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 84..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 112..115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 135..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..181
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 201..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 225..243
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 244..254
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 255..273
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 274..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 294..312
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 313..335
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 355..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 373..391
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 392..425
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 426..444
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 445..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 497 AA; 54844 MW; 348AE0D27960610C CRC64;
MQNLNKTEKT FFGQPRGLLT LFQTEFWERF SYYGMRAILV YYLYALTTAD NAGLGLPKAQ
AMAIVSIYGA LVYLSTIVGG WVADRLLGAS RTIFLGGILI TLGHIALATP FGLSSLFVAL
FLIILGTGML KPNISNMVGH LYSKDDSRRD TGFNIFVVGI NMGSLIAPLI VGTVGQGVNY
HLGFSLAAIG MIFALFAYWY GRLRHFPEIG REPSNPMDSK ARRNFLITLT IVVIVAIIGF
FLLYQASPAN FINNFINVLS IIGIVVPIIY FVMMFTSKKV ESDERRKLTA YIPLFLSAIV
FWAIEEQSST IIAVWGESRS NLDPTWFGIT FHIDPSWYQL LNPLFIVLLS PIFVRLWNKL
GERQPSTIVK FGLGLMLTGI SYLIMTLPGL LNGTSGRASA LWLVLMFAVQ MAGELLVSPV
GLSVSTKLAP VAFQSQMMAM WFLADSTSQA INAQITPLFK AATEVHFFAI TGIIGIIVGI
ILLIVKKPIL KLMGDVR
