DTPT_LACHE
ID DTPT_LACHE Reviewed; 497 AA.
AC O07380;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Di-/tripeptide transporter;
GN Name=dtpT;
OS Lactobacillus helveticus (Lactobacillus suntoryeus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15009 / DSM 20075 / BCRC 12936 / JCM 1120 / NBRC 15019 / NCIMB
RC 11971 / NRRL B-4526 / Lh12;
RX PubMed=9172341; DOI=10.1128/aem.63.6.2213-2217.1997;
RA Nakajima H., Hagting A., Kunji E.R.S., Poolman B., Konings W.N.;
RT "Cloning and functional expression in Escherichia coli of the gene encoding
RT the di- and tripeptide transport protein of Lactobacillus helveticus.";
RL Appl. Environ. Microbiol. 63:2213-2217(1997).
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}.
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DR EMBL; U77486; AAC45382.1; -; Genomic_DNA.
DR AlphaFoldDB; O07380; -.
DR SMR; O07380; -.
DR STRING; 326425.lhe_0332; -.
DR eggNOG; COG3104; Bacteria.
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 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; 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 membrane; Membrane; Peptide transport; Protein transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..497
FT /note="Di-/tripeptide transporter"
FT /id="PRO_0000064321"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 497 AA; 55469 MW; 69C064FF9A0A26A5 CRC64;
MRAILLFYMY YAVTKGGLGM SQTTAASIMS IYGSLVYLST LVGGWLSDRV WGSRKTVFYG
GVLIMLGHIV LALPAGVTVL YRSIALIVVG TGLLKPNVSD MVGGLYSVED PRRDAGFSIF
VFGINLGSII APWLVPWAAQ GFGVHIFGSQ LNFHAGFSLA AVGMFFGLVQ YVLGGKKYLS
TESLTPNDPI DKGDLLNVIK WVVIIIIAIV AILAAMAGVG QLSVDNVITL LTILAIALPI
YYFVMMFRSS KVTKIELGIH LLPVSLKNRL FFKKGYKRLK QIIQLELAIK RQSFIILIAL
IIMASILIPN KVIIAKHLLK LVLLVFYWIG LNLIPFSTFV LSFLFLDYIK HMFKKEGEQA
KKTKEKSRIH HGIEIPLFLR QLIINIFTLI ILEGETLFDE NGVEVNIAEH PVQGYTELNI
NLLNKDSIDL WADWIQSVAK YLLNIMYTAD VIVIIIFYLV KMAALWWAWS YIPLSTVFVG
YKYSGKDESL QAALEVL