ID   DPPC_ECOL6              Reviewed;         300 AA.
AC   P0AEG2; P37315;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Dipeptide transport system permease protein DppC {ECO:0000250|UniProtKB:P0AEG1};
GN   Name=dppC; OrderedLocusNames=c4357;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide
CC       transport. Responsible for the translocation of the substrate across
CC       the membrane. {ECO:0000250|UniProtKB:P0AEG1}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (DppD and
CC       DppF), two transmembrane proteins (DppB and DppC) and a solute-binding
CC       protein (DppA). {ECO:0000250|UniProtKB:P0AEG1}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AEG1}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82793.1; -; Genomic_DNA.
DR   RefSeq; WP_000084677.1; NC_004431.1.
DR   AlphaFoldDB; P0AEG2; -.
DR   STRING; 199310.c4357; -.
DR   EnsemblBacteria; AAN82793; AAN82793; c4357.
DR   GeneID; 66672570; -.
DR   KEGG; ecc:c4357; -.
DR   eggNOG; COG1173; Bacteria.
DR   HOGENOM; CLU_028518_1_1_6; -.
DR   OMA; VPTYFRM; -.
DR   BioCyc; ECOL199310:C4357-MON; -.
DR   Proteomes; UP000001410; 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:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR025966; OppC_N.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF12911; OppC_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 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..300
FT                   /note="Dipeptide transport system permease protein DppC"
FT                   /id="PRO_0000060011"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        53..101
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        123..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        158..206
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        228..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        252..265
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        287..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          98..287
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   300 AA;  32308 MW;  C4DD7BD82286EE62 CRC64;
     MSQVTENKVI SAPVPMTPLQ EFWHYFKRNK GAVVGLVYVV IVLFIAIFAN WIAPYNPAEQ
     FRDALLAPPA WQEGGSMAHL LGTDDVGRDV LSRLMYGARL SLLVGCLVVV LSLIMGVILG
     LIAGYFGGLV DNIIMRVVDI MLALPSLLLA LVLVAIFGPS IGNAALALTF VALPHYVRLT
     RAAVLVEVNR DYVTASRVAG AGAMRQMFIN IFPNCLAPLI VQASLGFSNA ILDMAALGFL
     GMGAQPPTPE WGTMLSDVLQ FAQSAWWVVT FPGLAILLTV LAFNLMGDGL RDALDPKLKQ