P23847 (DPPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Periplasmic dipeptide transport protein

Alternative name(s):
Dipeptide-binding protein
Short name=DBP

Gene names

Name:	dppA
Ordered Locus Names:	b3544, JW3513

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dipeptide-binding protein of a transport system that can be subject to osmotic shock. DppA is also required for peptide chemotaxis.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the bacterial solute-binding protein 5 family.

Ontologies

Keywords
Biological process	Chemotaxis Peptide transport Protein transport Transport
Cellular component	Periplasm
Domain	Signal
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ATP-binding cassette (ABC) transporter complex Inferred from sequence or structural similarity Ref.3. Source: EcoCyc outer membrane-bounded periplasmic space Inferred from experiment Ref.1. Source: EcoCyc
Molecular_function	dipeptide transporter activity Inferred from genetic interaction Ref.1. Source: EcoCyc peptide binding Inferred from direct assay PubMed 10537211. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Ref.2 Ref.7 Ref.8

Chain

29 – 535

507

Periplasmic dipeptide transport protein

PRO_0000031789

Amino acid modifications

Disulfide bond

34 ↔ 262

Ref.9

Disulfide bond

450 ↔ 463

Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

535

Helix Strand Turn

Details...

Beta strand

30 – 37

8

Helix

44 – 46

3

Helix

50 – 55

6

Helix

57 – 60

4

Beta strand

64 – 67

4

Beta strand

74 – 84

11

Beta strand

90 – 95

6

Helix

115 – 126

12

Turn

131 – 134

4

Helix

135 – 137

3

Helix

141 – 145

5

Helix

148 – 151

4

Beta strand

152 – 159

8

Beta strand

162 – 169

8

Helix

174 – 177

4

Helix

181 – 183

3

Helix

188 – 196

9

Helix

202 – 205

4

Beta strand

210 – 219

10

Turn

220 – 222

3

Beta strand

223 – 228

6

Beta strand

240 – 246

7

Helix

250 – 258

9

Helix

270 – 272

3

Helix

273 – 278

6

Beta strand

282 – 288

7

Beta strand

290 – 297

8

Turn

302 – 305

4

Helix

307 – 315

9

Helix

319 – 327

9

Beta strand

330 – 333

4

Beta strand

335 – 338

4

Helix

356 – 365

10

Beta strand

372 – 377

6

Helix

389 – 401

13

Turn

402 – 404

3

Beta strand

405 – 410

6

Helix

414 – 422

9

Beta strand

427 – 434

8

Beta strand

436 – 438

3

Helix

441 – 448

8

Helix

450 – 455

6

Helix

465 – 476

12

Helix

480 – 497

18

Beta strand

499 – 513

15

Beta strand

516 – 518

3

Sequences

	Sequence		Length	Mass (Da)
	P23847 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 3F7C4756EEA8C2F0	FASTA	535	60,294
	10 20 30 40 50 60 MRISLKKSGM LKLGLSLVAM TVAASVQAKT LVYCSEGSPE GFNPQLFTSG TTYDASSVPL 70 80 90 100 110 120 YNRLVEFKIG TTEVIPGLAE KWEVSEDGKT YTFHLRKGVK WHDNKEFKPT RELNADDVVF 130 140 150 160 170 180 SFDRQKNAQN PYHKVSGGSY EYFEGMGLPE LISEVKKVDD NTVQFVLTRP EAPFLADLAM 190 200 210 220 230 240 DFASILSKEY ADAMMKAGTP EKLDLNPIGT GPFQLQQYQK DSRIRYKAFD GYWGTKPQID 250 260 270 280 290 300 TLVFSITPDA SVRYAKLQKN ECQVMPYPNP ADIARMKQDK SINLMEMPGL NVGYLSYNVQ 310 320 330 340 350 360 KKPLDDVKVR QALTYAVNKD AIIKAVYQGA GVSAKNLIPP TMWGYNDDVQ DYTYDPEKAK 370 380 390 400 410 420 ALLKEAGLEK GFSIDLWAMP VQRPYNPNAR RMAEMIQADW AKVGVQAKIV TYEWGEYLKR 430 440 450 460 470 480 AKDGEHQTVM MGWTGDNGDP DNFFATLFSC AASEQGSNYS KWCYKPFEDL IQPARATDDH 490 500 510 520 530 NKRVELYKQA QVVMHDQAPA LIIAHSTVFE PVRKEVKGYV VDPLGKHHFE NVSIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein." Olson E.R., Dunyak D.S., Jurss L.M., Poorman R.A. J. Bacteriol. 173:234-244(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein." Abouhamad W.N., Manson M., Gibson M.M., Higgins C.F. Mol. Microbiol. 5:1035-1047(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-50. Strain: K12.
[3]	"The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression." Abouhamad W.N., Manson M.D. Mol. Microbiol. 14:1077-1092(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MM500.
[4]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-40. Strain: K12 / EMG2.
[8]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-32. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	Dunten P. Submitted (JUN-1995) to UniProtKB Cited for: DISULFIDE BONDS.
[10]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[11]	"Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis." Dunten P., Mowbray S.L. Protein Sci. 4:2327-2334(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[12]	"2-A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor." Nickitenko A.V., Trakhanov S., Quiocho F.A. Biochemistry 34:16585-16595(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M35045 Genomic DNA. Translation: AAA23707.1.
X58051 Genomic DNA. Translation: CAA41090.1.
L08399 Genomic DNA. Translation: AAA23702.1.
U00039 Genomic DNA. Translation: AAB18522.1.
U00096 Genomic DNA. Translation: AAC76569.1.
AP009048 Genomic DNA. Translation: BAE77750.1.

PIR

A39194.

RefSeq

NP_418001.1. NC_000913.2.
YP_491891.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DPE	X-ray	2.00	A	29-535	[»]
1DPP	X-ray	3.20	A/C/E/G	29-535	[»]

ProteinModelPortal

P23847.

SMR

P23847. Positions 29-535.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9467N.

IntAct

P23847. 5 interactions.

MINT

MINT-1240350.

STRING

511145.b3544.

2D gel databases

SWISS-2DPAGE

P23847.

Proteomic databases

PaxDb

P23847.

PRIDE

P23847.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76569; AAC76569; b3544.
BAE77750; BAE77750; BAE77750.

GeneID

12930534.
948062.

KEGG

ecj:Y75_p3632.
eco:b3544.

PATRIC

32122558. VBIEscCol129921_3657.

Organism-specific databases

EchoBASE

EB0244.

EcoGene

EG10248. dppA.

Phylogenomic databases

eggNOG

COG0747.

HOGENOM

HOG000164955.

KO

K12368.

OMA

GEHQAVM.

ProtClustDB

CLSK880713.

Enzyme and pathway databases

BioCyc

EcoCyc:DPPA-MONOMER.
ECOL316407:JW3513-MONOMER.

Gene expression databases

Genevestigator

P23847.

Family and domain databases

InterPro

IPR000914. SBP_bac_5.
IPR023765. SBP_bac_5_CS.
[Graphical view]

Pfam

PF00496. SBP_bac_5. 1 hit.
[Graphical view]

PROSITE

PS01040. SBP_BACTERIAL_5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23847.

Entry information

Entry name

DPPA_ECOLI

Accession

Primary (citable) accession number: P23847
Secondary accession number(s): Q2M7K6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program