DPPC_ECOLI
ID DPPC_ECOLI Reviewed; 300 AA.
AC P0AEG1; P37315; Q2M7K4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Dipeptide transport system permease protein DppC {ECO:0000305};
GN Name=dppC; OrderedLocusNames=b3542, JW3511;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=K12 / MM500;
RX PubMed=7536291; DOI=10.1111/j.1365-2958.1994.tb01340.x;
RA Abouhamad W.N., Manson M.D.;
RT "The dipeptide permease of Escherichia coli closely resembles other
RT bacterial transport systems and shows growth-phase-dependent expression.";
RL Mol. Microbiol. 14:1077-1092(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN 5-AMINOLEVULINIC ACID TRANSPORT.
RX PubMed=8444807; DOI=10.1128/jb.175.5.1452-1456.1993;
RA Verkamp E., Backman V.M., Bjoernsson J.M., Soell D., Eggertsson G.;
RT "The periplasmic dipeptide permease system transports 5-aminolevulinic acid
RT in Escherichia coli.";
RL J. Bacteriol. 175:1452-1456(1993).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP FUNCTION IN HEME TRANSPORT, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=16905647; DOI=10.1073/pnas.0605440103;
RA Letoffe S., Delepelaire P., Wandersman C.;
RT "The housekeeping dipeptide permease is the Escherichia coli heme
RT transporter and functions with two optional peptide binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12891-12896(2006).
CC -!- FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide
CC transport (PubMed:7536291). Responsible for the translocation of the
CC substrate across the membrane (Probable). {ECO:0000269|PubMed:7536291,
CC ECO:0000305}.
CC -!- FUNCTION: When a foreign outer membrane heme receptor is expressed in
CC E.coli, DppABCDF can also transport heme and its precursor, 5-
CC aminolevulinic acid (ALA), from the periplasm into the cytoplasm.
CC {ECO:0000269|PubMed:16905647, ECO:0000269|PubMed:8444807}.
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) (PubMed:7536291, PubMed:16905647). MppA can replace DppA
CC as binding protein for heme and ALA transport (PubMed:16905647).
CC {ECO:0000269|PubMed:16905647, ECO:0000269|PubMed:7536291}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene abolishes use of heme as
CC an iron source. {ECO:0000269|PubMed:16905647}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
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DR EMBL; L08399; AAA23704.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18520.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76567.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77752.1; -; Genomic_DNA.
DR PIR; S47764; S47764.
DR RefSeq; NP_417999.1; NC_000913.3.
DR RefSeq; WP_000084677.1; NZ_STEB01000018.1.
DR AlphaFoldDB; P0AEG1; -.
DR BioGRID; 4262184; 334.
DR ComplexPortal; CPX-4345; Heme/dipeptide ABC transporter complex, dppA variant.
DR ComplexPortal; CPX-4346; Heme/dipeptide ABC transporter complex, mppA variant.
DR DIP; DIP-9469N; -.
DR IntAct; P0AEG1; 2.
DR STRING; 511145.b3542; -.
DR jPOST; P0AEG1; -.
DR PaxDb; P0AEG1; -.
DR PRIDE; P0AEG1; -.
DR EnsemblBacteria; AAC76567; AAC76567; b3542.
DR EnsemblBacteria; BAE77752; BAE77752; BAE77752.
DR GeneID; 66672570; -.
DR GeneID; 948064; -.
DR KEGG; ecj:JW3511; -.
DR KEGG; eco:b3542; -.
DR PATRIC; fig|1411691.4.peg.3173; -.
DR EchoBASE; EB2510; -.
DR eggNOG; COG1173; Bacteria.
DR HOGENOM; CLU_028518_1_1_6; -.
DR InParanoid; P0AEG1; -.
DR OMA; VPTYFRM; -.
DR PhylomeDB; P0AEG1; -.
DR BioCyc; EcoCyc:DPPC-MON; -.
DR BioCyc; MetaCyc:DPPC-MON; -.
DR PRO; PR:P0AEG1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042938; P:dipeptide transport; IC:ComplexPortal.
DR GO; GO:0035351; P:heme transmembrane transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
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_0000060009"
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
