P0AEX9 (MALE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Maltose-binding periplasmic protein

Alternative name(s):
MBP
MMBP
Maltodextrin-binding protein

Gene names

Name:	malE
Ordered Locus Names:	b4034, JW3994

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	396 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	Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
Subcellular location	Periplasm.
Induction	Permanently repressed by cold shock in a PNPase-dependent fashion. Ref.11
Sequence similarities	Belongs to the bacterial solute-binding protein 1 family.

Ontologies

Keywords
Biological process	Sugar transport Transport
Cellular component	Periplasm
Domain	Signal
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	maltodextrin transport Inferred from mutant phenotype PubMed 6997044. Source: EcoCyc maltose transport Inferred from direct assay PubMed 2026607. Source: EcoCyc response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki
Cellular_component	ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Inferred from genetic interaction PubMed 2155217. Source: EcoliWiki periplasmic space Inferred from direct assay Ref.12. Source: EcoliWiki
Molecular_function	maltose transmembrane transporter activity Inferred from electronic annotation. Source: InterPro transporter activity Inferred from genetic interaction PubMed 2155217. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	3	EBI-369910,EBI-543750
malF	P02916	2	EBI-369910,EBI-1118919

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.8 Ref.9

Chain

27 – 396

370

Maltose-binding periplasmic protein

PRO_0000031694

Experimental info

Sequence conflict

36

1

W → A AA sequence Ref.8

Sequence conflict

46

1

L → H in CAA23581. Ref.5

Secondary structure

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396

Helix Strand Turn

Details...

Turn

28 – 31

4

Beta strand

32 – 36

5

Helix

39 – 41

3

Helix

43 – 57

15

Beta strand

60 – 64

5

Helix

69 – 76

8

Turn

77 – 80

4

Beta strand

84 – 89

6

Helix

90 – 92

3

Helix

93 – 98

6

Beta strand

99 – 101

3

Helix

109 – 112

4

Helix

117 – 122

6

Beta strand

123 – 125

3

Beta strand

126 – 129

4

Beta strand

131 – 137

7

Beta strand

140 – 144

5

Turn

145 – 147

3

Beta strand

148 – 150

3

Beta strand

153 – 155

3

Helix

158 – 166

9

Turn

167 – 169

3

Beta strand

171 – 173

3

Beta strand

177 – 179

3

Helix

180 – 189

10

Beta strand

193 – 198

6

Beta strand

201 – 208

8

Beta strand

209 – 211

3

Helix

212 – 226

15

Beta strand

227 – 230

4

Helix

236 – 244

9

Beta strand

248 – 253

6

Helix

255 – 257

3

Helix

258 – 263

6

Beta strand

268 – 271

4

Beta strand

275 – 279

5

Beta strand

284 – 293

10

Beta strand

294 – 297

4

Helix

299 – 308

10

Turn

309 – 311

3

Helix

313 – 322

10

Beta strand

327 – 330

4

Helix

331 – 337

7

Beta strand

338 – 340

3

Helix

341 – 352

12

Beta strand

353 – 355

3

Helix

362 – 377

16

Beta strand

379 – 381

3

Helix

383 – 392

10

Sequences

	Sequence		Length	Mass (Da)
	P0AEX9 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: A4C1B3C1777ADE47	FASTA	396	43,388
	10 20 30 40 50 60 MKIKTGARIL ALSALTTMMF SASALAKIEE GKLVIWINGD KGYNGLAEVG KKFEKDTGIK 70 80 90 100 110 120 VTVEHPDKLE EKFPQVAATG DGPDIIFWAH DRFGGYAQSG LLAEITPDKA FQDKLYPFTW 130 140 150 160 170 180 DAVRYNGKLI AYPIAVEALS LIYNKDLLPN PPKTWEEIPA LDKELKAKGK SALMFNLQEP 190 200 210 220 230 240 YFTWPLIAAD GGYAFKYENG KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE 250 260 270 280 290 300 AAFNKGETAM TINGPWAWSN IDTSKVNYGV TVLPTFKGQP SKPFVGVLSA GINAASPNKE 310 320 330 340 350 360 LAKEFLENYL LTDEGLEAVN KDKPLGAVAL KSYEEELAKD PRIAATMENA QKGEIMPNIP 370 380 390 QMSAFWYAVR TAVINAASGR QTVDEALKDA QTRITK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12." Duplay P., Bedouelle H., Fowler A., Zabin I., Saurin W., Hofnung M. J. Biol. Chem. 259:10606-10613(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[4]	"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.
[5]	"A DNA sequence containing the control regions of the malEFG and malK-lamB operons in Escherichia coli K12." Bedouelle H., Hofnung M. Mol. Gen. Genet. 185:82-87(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
[6]	"Promoters of the malEFG and malK-lamB operons in Escherichia coli K12." Bedouelle H., Schmeissner U., Hofnung M., Rosenberg M. J. Mol. Biol. 161:519-531(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
[7]	"The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli. Repeated DNA sequences are found in the malE-malF intercistronic region." Froshauer S., Beckwith J. J. Biol. Chem. 259:10896-10903(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 392-396.
[8]	"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 27-38. Strain: K12 / EMG2.
[9]	"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 27-30. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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]	"Changes in Escherichia coli transcriptome during acclimatization at low temperature." Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G., Deho G. Res. Microbiol. 154:573-580(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. Strain: K12 / MG1655 / ATCC 47076.
[12]	"The 2.3-A resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis." Spurlino J.C., Lu G.-Y., Quiocho F.A. J. Biol. Chem. 266:5202-5219(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[13]	"Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis." Sharff A.J., Rodseth L.E., Spurlino J.C., Quiocho F.A. Biochemistry 31:10657-10663(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[14]	"Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor." Quiocho F.A., Spurlino J.C., Rodseth L.E. Structure 5:997-1015(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[15]	"Redirecting the substrate specificity of heparan sulfate 2-O-sulfotransferase by structurally guided mutagenesis." Bethea H.N., Xu D., Liu J., Pedersen L.C. Proc. Natl. Acad. Sci. U.S.A. 105:18724-18729(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 27-392 IN COMPLEX WITH CHICKEN HS2ST1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00303 Genomic DNA. Translation: CAA23581.1.
U00006 Genomic DNA. Translation: AAC43128.1.
U00096 Genomic DNA. Translation: AAC77004.1.
AP009048 Genomic DNA. Translation: BAE78036.1.
J01648 Genomic DNA. Translation: AAB59056.1.
M16181 Genomic DNA. Translation: AAA24102.1.
M12635 Genomic DNA. Translation: AAA24123.1.
M12647 Genomic DNA. Translation: AAA24135.1.
M12650 Genomic DNA. Translation: AAA24138.1.
M12653 Genomic DNA. Translation: AAA24115.1.

PIR

JGECM. A03428.

RefSeq

NP_418458.1. NC_000913.2.
YP_492177.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A7L	X-ray	2.90	A/B/C	27-389	[»]
1ANF	X-ray	1.67	A	27-396	[»]
1DMB	X-ray	1.80	A	27-396	[»]
1EZ9	X-ray	1.90	A/B	27-396	[»]
1EZO	NMR	-	A	29-396	[»]
1EZP	NMR	-	A	29-396	[»]
1FQA	X-ray	1.90	A	28-396	[»]
1FQB	X-ray	1.90	A	28-396	[»]
1FQC	X-ray	2.30	A	28-396	[»]
1FQD	X-ray	2.30	A	28-396	[»]
1HSJ	X-ray	2.30	A/B	27-396	[»]
1IUD	X-ray	2.70	A	27-396	[»]
1JVX	X-ray	2.50	A	27-396	[»]
1JVY	X-ray	1.90	A	27-396	[»]
1JW4	X-ray	2.00	A	27-396	[»]
1JW5	X-ray	2.00	A	27-396	[»]
1LAX	X-ray	1.85	A/C	27-396	[»]
1LLS	X-ray	1.80	A	27-396	[»]
1MDP	X-ray	2.30	1/2	27-396	[»]
1MDQ	X-ray	1.90	A	27-396	[»]
1MG1	X-ray	2.50	A	31-392	[»]
1MH3	X-ray	2.10	A	27-392	[»]
1MH4	X-ray	2.30	A	27-392	[»]
1MPB	X-ray	2.00	A	27-396	[»]
1MPC	X-ray	2.10	A	27-396	[»]
1MPD	X-ray	2.30	A	27-396	[»]
1N3W	X-ray	2.60	A	27-396	[»]
1N3X	X-ray	2.50	A	27-396	[»]
1NL5	X-ray	2.10	A	27-396	[»]
1NMU	X-ray	2.31	A/C	27-392	[»]
1OMP	X-ray	1.80	A	27-396	[»]
1PEB	X-ray	2.60	A	27-396	[»]
1R6Z	X-ray	2.80	A/P/Z	27-392	[»]
1SVX	X-ray	2.24	B	29-392	[»]
1T0K	X-ray	3.24	A	29-392	[»]
1Y4C	X-ray	1.90	A	27-392	[»]
1YTV	X-ray	1.80	A/B	27-392	[»]
1ZIU	X-ray	2.00	A	27-396	[»]
1ZJL	X-ray	2.00	A	27-396	[»]
1ZKB	X-ray	2.20	A	27-396	[»]
1ZMG	X-ray	2.50	A	27-396	[»]
2D21	NMR	-	A	27-396	[»]
2H25	NMR	-	A	29-396	[»]
2KLF	NMR	-	A	29-396	[»]
2NVU	X-ray	2.80	B	25-392	[»]
2OBG	X-ray	2.35	A	31-396	[»]
2OK2	X-ray	2.00	A/B	28-392	[»]
2R6G	X-ray	2.80	E	27-396	[»]
2V93	NMR	-	A	27-396	[»]
2VGQ	X-ray	2.10	A	27-392	[»]
2XZ3	X-ray	1.95	A	27-392	[»]
2ZXT	X-ray	3.00	A	27-392	[»]
3A3C	X-ray	2.50	A	29-392	[»]
3C4M	X-ray	1.95	A/B	26-392	[»]
3CSB	X-ray	2.00	A	31-396	[»]
3CSG	X-ray	1.80	A	31-396	[»]
3DM0	X-ray	2.40	A	27-392	[»]
3EHS	X-ray	2.76	A	26-392	[»]
3EHT	X-ray	3.40	A	26-392	[»]
3EHU	X-ray	1.96	A/B	26-392	[»]
3F5F	X-ray	2.65	A	27-392	[»]
3G7V	X-ray	1.86	A/B/C/D	27-392	[»]
3G7W	X-ray	1.75	A	27-392	[»]
3H3G	X-ray	1.94	A	26-392	[»]
3H4Z	X-ray	2.35	A/B/C	27-392	[»]
3HPI	X-ray	2.00	A/B	26-396	[»]
3HST	X-ray	2.25	A/C	27-392	[»]
3IO4	X-ray	3.63	A/B/C	27-392	[»]
3IO6	X-ray	3.70	A/B/C	27-384	[»]
3IOR	X-ray	3.60	A/B/C	27-392	[»]
3IOT	X-ray	3.50	A/B/C	27-392	[»]
3IOU	X-ray	3.70	A/B/C	27-392	[»]
3IOV	X-ray	3.70	A/B/C	27-392	[»]
3IOW	X-ray	3.50	A/B/C	27-392	[»]
3KJT	X-ray	1.50	A	26-396	[»]
3L2J	X-ray	3.24	A/B	29-392	[»]
3LBS	X-ray	2.15	A/B	29-390	[»]
3LC8	X-ray	2.00	A/B	29-390	[»]
3MBP	X-ray	1.70	A	27-396	[»]
3MP1	X-ray	2.60	A	27-392	[»]
3MP6	X-ray	1.48	A	27-392	[»]
3MP8	X-ray	1.92	A	27-392	[»]
3MQ9	X-ray	2.80	A/B/C/D/E/F/G/H	27-395	[»]
3N94	X-ray	1.80	A	26-392	[»]
3O3U	X-ray	1.50	N	28-384	[»]
3OAI	X-ray	2.10	A/B	27-392	[»]
3OSQ	X-ray	1.90	A	27-396	[»]
3OSR	X-ray	2.00	A/B	27-396	[»]
3PGF	X-ray	2.10	A	27-392	[»]
3PUV	X-ray	2.40	E	27-396	[»]
3PUW	X-ray	2.30	E	27-396	[»]
3PUX	X-ray	2.30	E	27-396	[»]
3PUY	X-ray	3.10	E	27-396	[»]
3PUZ	X-ray	2.90	E	27-396	[»]
3PV0	X-ray	3.10	E	27-396	[»]
3PY7	X-ray	2.29	A	27-392	[»]
3Q25	X-ray	1.90	A	27-392	[»]
3Q26	X-ray	1.54	A	27-392	[»]
3Q27	X-ray	1.30	A	27-392	[»]
3Q28	X-ray	1.60	A	27-392	[»]
3Q29	X-ray	2.30	A/C	27-392	[»]
3RLF	X-ray	2.20	E	27-396	[»]
3RUM	X-ray	1.85	A	27-392	[»]
3SER	X-ray	2.35	A/C	27-392	[»]
3SES	X-ray	1.90	A/C	27-392	[»]
3SET	X-ray	1.90	A/C	27-392	[»]
3SEU	X-ray	1.85	A	27-392	[»]
3SEV	X-ray	3.05	A/C/E	27-392	[»]
3SEW	X-ray	1.55	A	27-392	[»]
3SEX	X-ray	1.95	A/C	27-392	[»]
3SEY	X-ray	1.85	A/C/E	27-392	[»]
3VFJ	X-ray	2.05	A	27-392	[»]
4B3N	X-ray	3.30	A/B	27-395	[»]
4DXB	X-ray	2.29	A/B	27-396	[»]
4DXC	X-ray	2.30	A	27-396	[»]
4EGC	X-ray	1.99	A	27-392	[»]
4EXK	X-ray	1.28	A	26-392	[»]
4FE8	X-ray	3.00	A/B/C	27-384	[»]
4FEB	X-ray	2.80	A/B/C	27-384	[»]
4FEC	X-ray	3.00	A/B/C	27-384	[»]
4FED	X-ray	2.81	A/B/C	27-384	[»]
4GIZ	X-ray	2.55	A/B	27-392	[»]
4GLI	X-ray	1.90	A	27-395	[»]
4MBP	X-ray	1.70	A	27-396	[»]

ProteinModelPortal

P0AEX9.

SMR

P0AEX9. Positions 27-392.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31871N.

IntAct

P0AEX9. 9 interactions.

STRING

511145.b4034.

Protein family/group databases

TCDB

3.A.1.1.1. ATP-binding cassette (ABC) superfamily.

2D gel databases

SWISS-2DPAGE

P0AEX9.

Proteomic databases

PaxDb

P0AEX9.

PRIDE

P0AEX9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77004; AAC77004; b4034.
BAE78036; BAE78036; BAE78036.

GeneID

12934071.
948538.

KEGG

ecj:Y75_p3921.
eco:b4034.

PATRIC

32123601. VBIEscCol129921_4149.

Organism-specific databases

EchoBASE

EB0549.

EcoGene

EG10554. malE.

Phylogenomic databases

eggNOG

COG2182.

HOGENOM

HOG000055250.

KO

K10108.

OMA

QDKLFPF.

ProtClustDB

PRK09474.

Enzyme and pathway databases

BioCyc

EcoCyc:MALE-MONOMER.
ECOL316407:JW3994-MONOMER.

Gene expression databases

Genevestigator

P0AEX9.

Family and domain databases

InterPro

IPR006060. Maltose-bd.
IPR006059. Solute-bd_1_bac.
IPR006061. Solute-bd_1_bac_CS.
[Graphical view]

Pfam

PF01547. SBP_bac_1. 1 hit.
[Graphical view]

PRINTS

PR00181. MALTOSEBP.

PROSITE

PS01037. SBP_BACTERIAL_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AEX9.

Entry information

Entry name

MALE_ECOLI

Accession

Primary (citable) accession number: P0AEX9
Secondary accession number(s): P02928, Q2M6S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program