DPPA_ECOLI
ID DPPA_ECOLI Reviewed; 535 AA.
AC P23847; Q2M7K6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Dipeptide-binding protein {ECO:0000303|PubMed:1702779, ECO:0000303|PubMed:1956284};
DE Short=DBP {ECO:0000303|PubMed:1956284};
DE AltName: Full=Periplasmic dipeptide transport protein {ECO:0000303|PubMed:1702779};
DE Flags: Precursor;
GN Name=dppA {ECO:0000303|PubMed:1702779, ECO:0000303|PubMed:1956284};
GN OrderedLocusNames=b3544, JW3513;
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, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=1702779; DOI=10.1128/jb.173.1.234-244.1991;
RA Olson E.R., Dunyak D.S., Jurss L.M., Poorman R.A.;
RT "Identification and characterization of dppA, an Escherichia coli gene
RT encoding a periplasmic dipeptide transport protein.";
RL J. Bacteriol. 173:234-244(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-50.
RC STRAIN=K12;
RX PubMed=1956284; DOI=10.1111/j.1365-2958.1991.tb01876.x;
RA Abouhamad W.N., Manson M., Gibson M.M., Higgins C.F.;
RT "Peptide transport and chemotaxis in Escherichia coli and Salmonella
RT typhimurium: characterization of the dipeptide permease (Dpp) and the
RT dipeptide-binding protein.";
RL Mol. Microbiol. 5:1035-1047(1991).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 29-61, FUNCTION, BINDING SPECIFICITY, AND DOMAIN.
RC STRAIN=K12;
RX PubMed=10537211; DOI=10.1099/00221287-145-10-2891;
RA Smith M.W., Tyreman D.R., Payne G.M., Marshall N.J., Payne J.W.;
RT "Substrate specificity of the periplasmic dipeptide-binding protein from
RT Escherichia coli: experimental basis for the design of peptide prodrugs.";
RL Microbiology 145:2891-2901(1999).
RN [8]
RP PROTEIN SEQUENCE OF 29-40.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 29-32.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [10]
RP FUNCTION.
RX PubMed=3520334; DOI=10.1038/321253a0;
RA Manson M.D., Blank V., Brade G., Higgins C.F.;
RT "Peptide chemotaxis in E. coli involves the Tap signal transducer and the
RT dipeptide permease.";
RL Nature 321:253-256(1986).
RN [11]
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 [12]
RP DISULFIDE BONDS.
RA Dunten P.;
RL Submitted (JUN-1995) to UniProtKB.
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [14]
RP FUNCTION IN HEME TRANSPORT, ACTIVITY REGULATION, 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).
RN [15] {ECO:0007744|PDB:1DPE}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-535, AND DOMAIN.
RX PubMed=8527431; DOI=10.1021/bi00051a006;
RA Nickitenko A.V., Trakhanov S., Quiocho F.A.;
RT "2-A resolution structure of DppA, a periplasmic dipeptide
RT transport/chemosensory receptor.";
RL Biochemistry 34:16585-16595(1995).
RN [16] {ECO:0007744|PDB:1DPP}
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 29-535 IN COMPLEX WITH DIPEPTIDE
RP GLY-LEU, FUNCTION, AND DOMAIN.
RX PubMed=8563629; DOI=10.1002/pro.5560041110;
RA Dunten P., Mowbray S.L.;
RT "Crystal structure of the dipeptide binding protein from Escherichia coli
RT involved in active transport and chemotaxis.";
RL Protein Sci. 4:2327-2334(1995).
CC -!- FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide
CC transport (PubMed:1702779, PubMed:7536291, PubMed:10537211). Binds
CC dipeptides and accepts a wide range of side chains, including small
CC neutral, bulky hydrophobic, and positively and negatively charged
CC groups (PubMed:10537211). Tripeptides are poor substrates
CC (PubMed:10537211). DppA alone controls the specificity of the Dpp
CC transporter (PubMed:10537211). In addition, plays a role in chemotaxis
CC toward peptides via interaction with the chemotaxis protein Tap
CC (PubMed:3520334, PubMed:8563629). {ECO:0000269|PubMed:10537211,
CC ECO:0000269|PubMed:1702779, ECO:0000269|PubMed:3520334,
CC ECO:0000269|PubMed:7536291, ECO:0000269|PubMed:8563629}.
CC -!- FUNCTION: Binds heme. When a foreign outer membrane heme receptor is
CC expressed in E.coli, DppABCDF can also transport heme and its
CC precursor, 5-aminolevulinic acid (ALA), from the periplasm into the
CC cytoplasm. {ECO:0000269|PubMed:16905647, ECO:0000269|PubMed:8444807}.
CC -!- ACTIVITY REGULATION: Heme binding is inhibited by dipeptide.
CC {ECO:0000269|PubMed:16905647}.
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:0000269|PubMed:7536291}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1702779}.
CC -!- INDUCTION: Expression is repressed by the presence of casamino acids.
CC {ECO:0000269|PubMed:1702779}.
CC -!- DOMAIN: Consists of two distinct domains (I and II) connected by two
CC strands that presumably function as a hinge (PubMed:8527431,
CC PubMed:8563629). Undergoes conformational change upon substrate binding
CC (PubMed:10537211). {ECO:0000269|PubMed:10537211,
CC ECO:0000269|PubMed:8527431, ECO:0000269|PubMed:8563629}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene results in the inability
CC of a proline auxotroph to utilize Pro-Gly as a proline source
CC (PubMed:1702779). Inactivation of the gene has no effect on iron-heme
CC utilization, but the double mppA dppA mutant is unable to use heme as
CC iron source (PubMed:16905647). {ECO:0000269|PubMed:16905647,
CC ECO:0000269|PubMed:1702779}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; M35045; AAA23707.1; -; Genomic_DNA.
DR EMBL; X58051; CAA41090.1; -; Genomic_DNA.
DR EMBL; L08399; AAA23702.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18522.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76569.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77750.1; -; Genomic_DNA.
DR PIR; A39194; A39194.
DR RefSeq; NP_418001.1; NC_000913.3.
DR RefSeq; WP_001222883.1; NZ_STEB01000018.1.
DR PDB; 1DPE; X-ray; 2.00 A; A=29-535.
DR PDB; 1DPP; X-ray; 3.20 A; A/C/E/G=29-535.
DR PDBsum; 1DPE; -.
DR PDBsum; 1DPP; -.
DR AlphaFoldDB; P23847; -.
DR SMR; P23847; -.
DR BioGRID; 4259528; 228.
DR ComplexPortal; CPX-4345; Heme/dipeptide ABC transporter complex, dppA variant.
DR DIP; DIP-9467N; -.
DR IntAct; P23847; 6.
DR STRING; 511145.b3544; -.
DR SWISS-2DPAGE; P23847; -.
DR jPOST; P23847; -.
DR PaxDb; P23847; -.
DR PRIDE; P23847; -.
DR EnsemblBacteria; AAC76569; AAC76569; b3544.
DR EnsemblBacteria; BAE77750; BAE77750; BAE77750.
DR GeneID; 66672568; -.
DR GeneID; 948062; -.
DR KEGG; ecj:JW3513; -.
DR KEGG; eco:b3544; -.
DR PATRIC; fig|1411691.4.peg.3170; -.
DR EchoBASE; EB0244; -.
DR eggNOG; COG0747; Bacteria.
DR HOGENOM; CLU_017028_7_0_6; -.
DR InParanoid; P23847; -.
DR OMA; YIAYNVM; -.
DR PhylomeDB; P23847; -.
DR BioCyc; EcoCyc:DPPA-MON; -.
DR BioCyc; MetaCyc:DPPA-MON; -.
DR EvolutionaryTrace; P23847; -.
DR PRO; PR:P23847; -.
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:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0020037; F:heme binding; IPI:EcoCyc.
DR GO; GO:0042277; F:peptide binding; IDA:EcoCyc.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0042938; P:dipeptide transport; IMP:EcoCyc.
DR GO; GO:0035351; P:heme transmembrane transport; IC:ComplexPortal.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Direct protein sequencing; Disulfide bond;
KW Peptide transport; Periplasm; Protein transport; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:1956284,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841"
FT CHAIN 29..535
FT /note="Dipeptide-binding protein"
FT /id="PRO_0000031789"
FT BINDING 48..50
FT /ligand="glycyl-L-leucine"
FT /ligand_id="ChEBI:CHEBI:143163"
FT /evidence="ECO:0000269|PubMed:8563629,
FT ECO:0007744|PDB:1DPP"
FT BINDING 383..385
FT /ligand="glycyl-L-leucine"
FT /ligand_id="ChEBI:CHEBI:143163"
FT /evidence="ECO:0000269|PubMed:8563629,
FT ECO:0007744|PDB:1DPP"
FT BINDING 433..436
FT /ligand="glycyl-L-leucine"
FT /ligand_id="ChEBI:CHEBI:143163"
FT /evidence="ECO:0000269|PubMed:8563629,
FT ECO:0007744|PDB:1DPP"
FT DISULFID 34..262
FT /evidence="ECO:0000269|Ref.12"
FT DISULFID 450..463
FT /evidence="ECO:0000269|Ref.12"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:1DPE"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:1DPE"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:1DPE"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 389..401
FT /evidence="ECO:0007829|PDB:1DPE"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 441..448
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 465..476
FT /evidence="ECO:0007829|PDB:1DPE"
FT HELIX 480..497
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 499..513
FT /evidence="ECO:0007829|PDB:1DPE"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:1DPE"
SQ SEQUENCE 535 AA; 60294 MW; 3F7C4756EEA8C2F0 CRC64;
MRISLKKSGM LKLGLSLVAM TVAASVQAKT LVYCSEGSPE GFNPQLFTSG TTYDASSVPL
YNRLVEFKIG TTEVIPGLAE KWEVSEDGKT YTFHLRKGVK WHDNKEFKPT RELNADDVVF
SFDRQKNAQN PYHKVSGGSY EYFEGMGLPE LISEVKKVDD NTVQFVLTRP EAPFLADLAM
DFASILSKEY ADAMMKAGTP EKLDLNPIGT GPFQLQQYQK DSRIRYKAFD GYWGTKPQID
TLVFSITPDA SVRYAKLQKN ECQVMPYPNP ADIARMKQDK SINLMEMPGL NVGYLSYNVQ
KKPLDDVKVR QALTYAVNKD AIIKAVYQGA GVSAKNLIPP TMWGYNDDVQ DYTYDPEKAK
ALLKEAGLEK GFSIDLWAMP VQRPYNPNAR RMAEMIQADW AKVGVQAKIV TYEWGEYLKR
AKDGEHQTVM MGWTGDNGDP DNFFATLFSC AASEQGSNYS KWCYKPFEDL IQPARATDDH
NKRVELYKQA QVVMHDQAPA LIIAHSTVFE PVRKEVKGYV VDPLGKHHFE NVSIE
