DPPC_ECO57
ID DPPC_ECO57 Reviewed; 300 AA.
AC P0AEG3; P37315;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Dipeptide transport system permease protein DppC {ECO:0000250|UniProtKB:P0AEG1};
GN Name=dppC; OrderedLocusNames=Z4959, ECs4422;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG58686.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37845.1; -; Genomic_DNA.
DR PIR; B86028; B86028.
DR PIR; F91181; F91181.
DR RefSeq; NP_312449.1; NC_002695.1.
DR RefSeq; WP_000084677.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEG3; -.
DR STRING; 155864.EDL933_4800; -.
DR PRIDE; P0AEG3; -.
DR EnsemblBacteria; AAG58686; AAG58686; Z4959.
DR EnsemblBacteria; BAB37845; BAB37845; ECs_4422.
DR GeneID; 66672570; -.
DR GeneID; 915715; -.
DR KEGG; ece:Z4959; -.
DR KEGG; ecs:ECs_4422; -.
DR PATRIC; fig|386585.9.peg.4626; -.
DR eggNOG; COG1173; Bacteria.
DR HOGENOM; CLU_028518_1_1_6; -.
DR OMA; VPTYFRM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..300
FT /note="Dipeptide transport system permease protein DppC"
FT /id="PRO_0000060010"
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