ECOLI:MALE

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	malE
Protein Name(s)	Maltose-binding periplasmic protein MBP MMBP Maltodextrin-binding protein
External Links
UniProt	P0AEX9
EMBL	V00303 U00006 U00096 AP009048 J01648 M16181 M12635 M12647 M12650 M12653
PIR	A03428
RefSeq	NP_418458.1 YP_492177.1
PDB	1A7L 1ANF 1DMB 1EZ9 1EZO 1EZP 1FQA 1FQB 1FQC 1FQD 1HSJ 1IUD 1JVX 1JVY 1JW4 1JW5 1LAX 1LLS 1MDP 1MDQ 1MG1 1MH3 1MH4 1MPB 1MPC 1MPD 1N3W 1N3X 1NL5 1NMU 1OMP 1PEB 1R6Z 1SVX 1T0K 1Y4C 1YTV 1ZIU 1ZJL 1ZKB 1ZMG 2D21 2H25 2KLF 2NVU 2OBG 2OK2 2R6G 2V93 2VGQ 2XZ3 2ZXT 3A3C 3C4M 3CSB 3CSG 3DM0 3EHS 3EHT 3EHU 3F5F 3G7V 3G7W 3H3G 3H4Z 3HPI 3HST 3IO4 3IO6 3IOR 3IOT 3IOU 3IOV 3IOW 3KJT 3L2J 3LBS 3LC8 3MBP 3MP1 3MP6 3MP8 3MQ9 3N94 3O3U 3OAI 3OSQ 3OSR 3PGF 3PUV 3PUW 3PUX 3PUY 3PUZ 3PV0 3PY7 3Q25 3Q26 3Q27 3Q28 3Q29 3RLF 3RUM 3SER 3SES 3SET 3SEU 3SEV 3SEW 3SEX 3SEY 3VFJ 3W15 3WAI 4B3N 4BL8 4BL9 4BLA 4BLB 4BLD 4DXB 4DXC 4EDQ 4EGC 4EXK 4FE8 4FEB 4FEC 4FED 4GIZ 4GLI 4IFP 4IKM 4IRL 4JBZ 4JKM 4KEG 4KHZ 4KI0 4KV3 4KYC 4KYD 4KYE 4MBP 4N4X 4NDZ 4R0Y
PDBsum	1A7L 1ANF 1DMB 1EZ9 1EZO 1EZP 1FQA 1FQB 1FQC 1FQD 1HSJ 1IUD 1JVX 1JVY 1JW4 1JW5 1LAX 1LLS 1MDP 1MDQ 1MG1 1MH3 1MH4 1MPB 1MPC 1MPD 1N3W 1N3X 1NL5 1NMU 1OMP 1PEB 1R6Z 1SVX 1T0K 1Y4C 1YTV 1ZIU 1ZJL 1ZKB 1ZMG 2D21 2H25 2KLF 2NVU 2OBG 2OK2 2R6G 2V93 2VGQ 2XZ3 2ZXT 3A3C 3C4M 3CSB 3CSG 3DM0 3EHS 3EHT 3EHU 3F5F 3G7V 3G7W 3H3G 3H4Z 3HPI 3HST 3IO4 3IO6 3IOR 3IOT 3IOU 3IOV 3IOW 3KJT 3L2J 3LBS 3LC8 3MBP 3MP1 3MP6 3MP8 3MQ9 3N94 3O3U 3OAI 3OSQ 3OSR 3PGF 3PUV 3PUW 3PUX 3PUY 3PUZ 3PV0 3PY7 3Q25 3Q26 3Q27 3Q28 3Q29 3RLF 3RUM 3SER 3SES 3SET 3SEU 3SEV 3SEW 3SEX 3SEY 3VFJ 3W15 3WAI 4B3N 4BL8 4BL9 4BLA 4BLB 4BLD 4DXB 4DXC 4EDQ 4EGC 4EXK 4FE8 4FEB 4FEC 4FED 4GIZ 4GLI 4IFP 4IKM 4IRL 4JBZ 4JKM 4KEG 4KHZ 4KI0 4KV3 4KYC 4KYD 4KYE 4MBP 4N4X 4NDZ 4R0Y
ProteinModelPortal	P0AEX9
SMR	P0AEX9
BioGrid	852832
DIP	DIP-31871N
IntAct	P0AEX9
STRING	511145.b4034
TCDB	3.A.1.1.1
SWISS-2DPAGE	P0AEX9
PaxDb	P0AEX9
PRIDE	P0AEX9
EnsemblBacteria	AAC77004 BAE78036
GeneID	12934071 948538
KEGG	ecj:Y75_p3921 eco:b4034
PATRIC	32123601
EchoBASE	EB0549
EcoGene	EG10554
eggNOG	COG2182
HOGENOM	HOG000055250
InParanoid	P0AEX9
KO	K10108
OMA	WAWANID
OrthoDB	EOG6CCH2B
PhylomeDB	P0AEX9
BioCyc	EcoCyc:MALE-MONOMER ECOL316407:JW3994-MONOMER MetaCyc:MALE-MONOMER
EvolutionaryTrace	P0AEX9
PRO	PR:P0AEX9
Proteomes	UP000000318 UP000000625
Genevestigator	P0AEX9
GO	GO:0043190 GO:0055052 GO:1990060 GO:0030288 GO:0042597 GO:1901982 GO:0005363 GO:0005215 GO:0008643 GO:0060326 GO:0006974 GO:0034289 GO:0042956 GO:0015768 GO:0006810
InterPro	IPR006060 IPR006061 IPR006059
Pfam	PF01547
PRINTS	PR00181
PROSITE	PS01037

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:1990060	maltose transport complex	PMID:22286990^[1]	ECO:0000314			C	Figure 7	complete CACAO 8760
part_of	GO:0055052	ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing	PMID:2155217^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	EcoliWiki:lamB EcoliWiki:malF EcoliWiki:malG EcoliWiki:malK	C	Seeded From UniProt	complete
part_of	GO:0043190	ATP-binding cassette (ABC) transporter complex	PMID:2155217^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	EcoliWiki:lamB EcoliWiki:malF EcoliWiki:malG EcoliWiki:malK	C	Seeded From UniProt	complete
part_of	GO:0042597	periplasmic space	PMID:15117946^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0015768	maltose transport	PMID:2155217^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	EcoliWiki:lamB EcoliWiki:malF EcoliWiki:malG EcoliWiki:malK	P	Seeded From UniProt	complete
involved_in	GO:0008643	carbohydrate transport	PMID:2155217^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	EcoliWiki:lamB EcoliWiki:malF EcoliWiki:malG EcoliWiki:malK	P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:11967071^[4]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0005215	transporter activity	PMID:2155217^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	EcoliWiki:lamB EcoliWiki:malF EcoliWiki:malG EcoliWiki:malK	F	Seeded From UniProt	complete
enables	GO:1901982	maltose binding	PMID:4215651^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:1901982	maltose binding	PMID:2002054^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0060326	cell chemotaxis	PMID:1429629^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0060326	cell chemotaxis	PMID:1091624^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042956	maltodextrin transport	PMID:6997044^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0034289	detection of maltose stimulus	PMID:1429629^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0034289	detection of maltose stimulus	PMID:1091624^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:4215651^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:24140104^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:2002054^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:15911532^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0015768	maltose transport	PMID:7040366^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0015768	maltose transport	PMID:6997044^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0015768	maltose transport	PMID:2155217^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0015768	maltose transport	PMID:2026607^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0034219	carbohydrate transmembrane transport	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0015144	P	Seeded From UniProt	complete
involved_in	GO:0008643	carbohydrate transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006060	P	Seeded From UniProt	complete
enables	GO:0015144	carbohydrate transmembrane transporter activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006060	F	Seeded From UniProt	complete
involved_in	GO:0055085	transmembrane transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006061	P	Seeded From UniProt	complete
part_of	GO:0042597	periplasmic space	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0574 UniProtKB-SubCell:SL-0200	C	Seeded From UniProt	complete
involved_in	GO:0008643	carbohydrate transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0762	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Sedlak, RH et al. (2012) Engineered Escherichia coli silver-binding periplasmic protein that promotes silver tolerance. Appl. Environ. Microbiol. 78 2289-96 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Davidson, AL & Nikaido, H (1990) Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli. J. Biol. Chem. 265 4254-60 PubMed GONUTS page
↑ Austermuhle, MI et al. (2004) Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport. J. Biol. Chem. 279 28243-50 PubMed GONUTS page
↑ Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
↑ ^5.0 ^5.1 Kellermann, O & Szmelcman, S (1974) Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein. Eur. J. Biochem. 47 139-49 PubMed GONUTS page
↑ ^6.0 ^6.1 Spurlino, JC et al. (1991) The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266 5202-19 PubMed GONUTS page
↑ ^7.0 ^7.1 Zhang, Y et al. (1992) Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein. J. Biol. Chem. 267 22813-20 PubMed GONUTS page
↑ ^8.0 ^8.1 Hazelbauer, GL (1975) Maltose chemoreceptor of Escherichia coli. J. Bacteriol. 122 206-14 PubMed GONUTS page
↑ ^9.0 ^9.1 Ferenci, T (1980) The recognition of maltodextrins by Escherichia coli. Eur. J. Biochem. 108 631-6 PubMed GONUTS page
↑ Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ Shuman, HA (1982) Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane. J. Biol. Chem. 257 5455-61 PubMed GONUTS page
↑ Davidson, AL & Nikaido, H (1991) Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli. J. Biol. Chem. 266 8946-51 PubMed GONUTS page

[PMID:22286990-1] Sedlak, RH et al. (2012) Engineered Escherichia coli silver-binding periplasmic protein that promotes silver tolerance. Appl. Environ. Microbiol. 78 2289-96 PubMed GONUTS page

[PMID:2155217-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Davidson, AL & Nikaido, H (1990) Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli. J. Biol. Chem. 265 4254-60 PubMed GONUTS page

[PMID:15117946-3] Austermuhle, MI et al. (2004) Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport. J. Biol. Chem. 279 28243-50 PubMed GONUTS page

[PMID:11967071-4] Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page

[PMID:4215651-5] 5.0 ^5.1 Kellermann, O & Szmelcman, S (1974) Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein. Eur. J. Biochem. 47 139-49 PubMed GONUTS page

[PMID:2002054-6] 6.0 ^6.1 Spurlino, JC et al. (1991) The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266 5202-19 PubMed GONUTS page

[PMID:1429629-7] 7.0 ^7.1 Zhang, Y et al. (1992) Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein. J. Biol. Chem. 267 22813-20 PubMed GONUTS page

[PMID:1091624-8] 8.0 ^8.1 Hazelbauer, GL (1975) Maltose chemoreceptor of Escherichia coli. J. Bacteriol. 122 206-14 PubMed GONUTS page

[PMID:6997044-9] 9.0 ^9.1 Ferenci, T (1980) The recognition of maltodextrins by Escherichia coli. Eur. J. Biochem. 108 631-6 PubMed GONUTS page

[PMID:24140104-10] Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 PubMed GONUTS page

[PMID:15911532-11] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:7040366-12] Shuman, HA (1982) Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane. J. Biol. Chem. 257 5455-61 PubMed GONUTS page

[PMID:2026607-13] Davidson, AL & Nikaido, H (1991) Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli. J. Biol. Chem. 266 8946-51 PubMed GONUTS page

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ECOLI:MALE

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