DTPA_SALTY
ID DTPA_SALTY Reviewed; 501 AA.
AC Q8ZPM6;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=STM1452;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION.
RC STRAIN=LT2;
RX PubMed=6090406; DOI=10.1128/jb.160.1.122-130.1984;
RA Gibson M.M., Price M., Higgins C.F.;
RT "Genetic characterization and molecular cloning of the tripeptide permease
RT (tpp) genes of Salmonella typhimurium.";
RL J. Bacteriol. 160:122-130(1984).
RN [3]
RP INDUCTION.
RC STRAIN=LT2;
RX PubMed=3037276; DOI=10.1007/bf00331499;
RA Gibson M.M., Ellis E.M., Graeme-Cook K.A., Higgins C.F.;
RT "OmpR and EnvZ are pleiotropic regulatory proteins: positive regulation of
RT the tripeptide permease (tppB) of Salmonella typhimurium.";
RL Mol. Gen. Genet. 207:120-129(1987).
CC -!- FUNCTION: Proton-dependent permease that transports di- and
CC tripeptides. {ECO:0000255|HAMAP-Rule:MF_01878,
CC ECO:0000269|PubMed:6090406}.
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 -!- INDUCTION: Transcriptionally activated by the EnvZ/OmpR regulatory
CC system. Strongly stimulated under anaerobic conditions through an OmpR-
CC independent mechanism. {ECO:0000269|PubMed:3037276}.
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; AE006468; AAL20374.1; -; Genomic_DNA.
DR RefSeq; NP_460415.1; NC_003197.2.
DR RefSeq; WP_000100911.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPM6; -.
DR SMR; Q8ZPM6; -.
DR STRING; 99287.STM1452; -.
DR PaxDb; Q8ZPM6; -.
DR EnsemblBacteria; AAL20374; AAL20374; STM1452.
DR GeneID; 1252970; -.
DR KEGG; stm:STM1452; -.
DR PATRIC; fig|99287.12.peg.1535; -.
DR HOGENOM; CLU_004790_0_0_6; -.
DR OMA; QMMGVWF; -.
DR PhylomeDB; Q8ZPM6; -.
DR BioCyc; SENT99287:STM1452-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015333; F:peptide:proton symporter activity; IBA:GO_Central.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..501
FT /note="Dipeptide and tripeptide permease A"
FT /id="PRO_0000064327"
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..383
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 405..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..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
SQ SEQUENCE 501 AA; 54340 MW; 2F0AF797B39AB862 CRC64;
MSTANKKPTE SVSLNAFKQP KAFYLIFSIE LWERFGYYGL QGIMAVYLVK QLGMSEADSI
TLFSSFSALV YGLVAIGGWL GDKILGTKRV IMLGAVVLAI GYALVAWSGH DAGIVYMGMA
AIAVGNGLFK ANPSSLLSTC YAKDDPRLDG AFTMYYMSVN IGSFFSMLAT PWLAARYGWS
TAFALSVVGM LITVVNFAFC QRWVKSYGSK PDFEPINFRN LLLTIVGIVV LIAVATWLLH
NQDIARMVLG VIALGIVIIF GKEAFSMHGA ARRKMIVAFI LMLQAIIFFV LYSQMPTSLN
FFAIRNVEHS ILGIAFEPEQ YQALNPFWII IGSPILAAIY NRMGDTLPMP MKFAIGMVLC
SGAFLILPLG AKFANDAGIV SVNWLIASYG LQSIGELMIS GLGLAMVAQL VPQRLMGFIM
GSWFLTTAGA NIIGGYVANL MAVPSDVTDP LMSLEVYGRV FMQIGIATAV IAVLMLLTAP
KLNRMTQDDD TAEKGSKAAT V
