DPPF_ECOLI
ID DPPF_ECOLI Reviewed; 334 AA.
AC P37313; Q2M7K2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Dipeptide transport ATP-binding protein DppF {ECO:0000305};
DE EC=7.4.2.9 {ECO:0000305|PubMed:7536291};
GN Name=dppF; Synonyms=dppE; OrderedLocusNames=b3540, JW3509;
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, CATALYTIC ACTIVITY, AND
RP 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 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 energy coupling to the
CC transport system (Probable). {ECO:0000269|PubMed:7536291, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23120, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90799, ChEBI:CHEBI:456216; EC=7.4.2.9;
CC Evidence={ECO:0000305|PubMed:7536291};
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 {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
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 ABC transporter superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L08399; AAA23706.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18518.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76565.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77754.1; -; Genomic_DNA.
DR PIR; S47762; S47762.
DR RefSeq; NP_417997.1; NC_000913.3.
DR RefSeq; WP_000107012.1; NZ_SSZK01000039.1.
DR AlphaFoldDB; P37313; -.
DR SMR; P37313; -.
DR BioGRID; 4259468; 339.
DR BioGRID; 852364; 3.
DR ComplexPortal; CPX-4345; Heme/dipeptide ABC transporter complex, dppA variant.
DR ComplexPortal; CPX-4346; Heme/dipeptide ABC transporter complex, mppA variant.
DR IntAct; P37313; 17.
DR STRING; 511145.b3540; -.
DR jPOST; P37313; -.
DR PaxDb; P37313; -.
DR PRIDE; P37313; -.
DR EnsemblBacteria; AAC76565; AAC76565; b3540.
DR EnsemblBacteria; BAE77754; BAE77754; BAE77754.
DR GeneID; 948056; -.
DR KEGG; ecj:JW3509; -.
DR KEGG; eco:b3540; -.
DR PATRIC; fig|1411691.4.peg.3175; -.
DR EchoBASE; EB2512; -.
DR eggNOG; COG4608; Bacteria.
DR HOGENOM; CLU_000604_1_23_6; -.
DR InParanoid; P37313; -.
DR OMA; GRYPHMF; -.
DR PhylomeDB; P37313; -.
DR BioCyc; EcoCyc:DPPF-MON; -.
DR BioCyc; MetaCyc:DPPF-MON; -.
DR PRO; PR:P37313; -.
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:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0015232; F:heme transmembrane transporter activity; IMP:EcoliWiki.
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 GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013563; Oligopep_ABC_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08352; oligo_HPY; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Peptide transport; Protein transport;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..334
FT /note="Dipeptide transport ATP-binding protein DppF"
FT /id="PRO_0000092317"
FT DOMAIN 13..262
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 320..334
FT /note="LVACFAVDQDENPQR -> RNDDKSADRQSQHA (in Ref. 1;
FT AAA23706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37560 MW; 4E5619914955CA51 CRC64;
MSTQEATLQQ PLLQAIDLKK HYPVKKGMFA PERLVKALDG VSFNLERGKT LAVVGESGCG
KSTLGRLLTM IEMPTGGELY YQGQDLLKHD PQAQKLRRQK IQIVFQNPYG SLNPRKKVGQ
ILEEPLLINT SLSKEQRREK ALSMMAKVGL KTEHYDRYPH MFSGGQRQRI AIARGLMLDP
DVVIADEPVS ALDVSVRAQV LNLMMDLQQE LGLSYVFISH DLSVVEHIAD EVMVMYLGRC
VEKGTKDQIF NNPRHPYTQA LLSATPRLNP DDRRERIKLS GELPSPLNPP PGCAFNARCR
RRFGPCTQLQ PQLKDYGGQL VACFAVDQDE NPQR
