DTPA_CROTZ
ID DTPA_CROTZ Reviewed; 499 AA.
AC C9Y3M8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Dipeptide and tripeptide permease A {ECO:0000255|HAMAP-Rule:MF_01878};
GN Name=dtpA {ECO:0000255|HAMAP-Rule:MF_01878}; OrderedLocusNames=Ctu_20000;
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX PubMed=21037008; DOI=10.1128/jb.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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 -!- SEQUENCE CAUTION:
CC Sequence=CBA30607.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FN543093; CBA30607.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041924163.1; NC_013282.2.
DR AlphaFoldDB; C9Y3M8; -.
DR SMR; C9Y3M8; -.
DR EnsemblBacteria; CBA30607; CBA30607; CTU_20000.
DR GeneID; 60372694; -.
DR KEGG; ctu:CTU_20000; -.
DR PATRIC; fig|693216.3.peg.1891; -.
DR HOGENOM; CLU_004790_0_0_6; -.
DR Proteomes; UP000002069; 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..499
FT /note="Dipeptide and tripeptide permease A"
FT /id="PRO_0000395174"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 56..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..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 239..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..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 372..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..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
SQ SEQUENCE 499 AA; 54335 MW; FCDFACD35087206D CRC64;
MSTANKKPAE SVSMNAFKQP RSFYLIFSIE LWERFGFYGL QGIMAVYLVK QLGMSEADSI
TLFSSFSALV YGLVAIGGWL GDKVLGTKRV IMLGTIVLAI GYALVAWSGH DAAIVYFGMA
TIAVGNGLFK ANPSALLSTC YEKDDPRLDG AFTMYYMAIN IGSFFSMLAT PWLAEKFGWS
VAFSLSFVGM LITLVNFIFC KKWVKDYGSK PDFAPLHVGK LLATIVGIVV LVAIATWLLH
NQGIARLVLG VVALGIVIIF AKEAFAMQGA ARRKMIVAFI LMLEAIVFFV LYQQMPTSLN
FFAIRNVEHS ILGIAFQPEQ FQALNPFWIM IGSPILAAIY NKMGDRLPMP FKFTIGMLLC
SGAFLVLPLG AKFASEAGIV SVNWLILSYA LQSIGELMIS GLGLAMVAQL VPQRLMGFIM
GSWFLTTAGA AMIAGKVANL MAVPENVSDP LQSLEVYGRV FMQIGIATGV IAVLMLLTAP
LLNRMTQEDK PKETDTAHA
