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Escherichia coli K-12 substr. MG1655 Transporter: MalX PTS permease



Gene: malX Accession Numbers: EG10563 (EcoCyc), b1621, ECK1616

Synonyms: EIIBCmalX, Enzyme IIBCmalX

Regulation Summary Diagram: ?

Summary:
The deduced amino acid sequence of MalX displays 35% identity with PtsG (Enzyme IIBCglc of the glucose PTS). The constitutive expression of chromosomal malX (through a malI::Tn10 mutation) restores growth on glucose in an E. coli ΔptsG ΔptsM strain provided cytoplasmic glucokinase (encoded by glk) is present. This suggests that the MalX protein can transport glucose via facilitated diffusion [Reidl91]. Overexpression of malX from a plasmid restores growth on glucose in a ΔptsG ΔptsM Δglk strain which suggests that MalX also functions, albeit inefficiently, in vectorial phosphorylation of glucose possibly in conjunction with Crr (Enzyme IIAglc) [Reidl91]. MalX may also transport maltose by facilitated diffusion [Reidl91]. The physiological function of MalX is not clear [Reidl91]. MalX/Crr is a member of the PTS Glucose-Glucoside family of transporters [Saier14].

malX forms an operon with malY. MalI regulates the expression of malXY. Putative MalI binding sites have been identified in the intergenic malI-malX region [Reidl91].

malX is a virulence associated gene in E. coli strains causing extraintestinal infections [Guyer98, Ostblom11].

Citations: [Postma93]

Gene Citations: [Otsuka96]

Locations: inner membrane

Map Position: [1,697,379 -> 1,698,971] (36.58 centisomes)
Length: 1593 bp / 530 aa

Molecular Weight of Polypeptide: 56.627 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0005429 , CGSC:32254 , DIP:DIP-10150N , EchoBASE:EB0558 , EcoGene:EG10563 , EcoliWiki:b1621 , Mint:MINT-1239961 , ModBase:P19642 , OU-Microarray:b1621 , PortEco:malX , PR:PRO_000023156 , Pride:P19642 , Protein Model Portal:P19642 , RefSeq:NP_416138 , RegulonDB:EG10563 , SMR:P19642 , String:511145.b1621 , UniProt:P19642

Relationship Links: InterPro:IN-FAMILY:IPR001996 , InterPro:IN-FAMILY:IPR003352 , InterPro:IN-FAMILY:IPR004719 , InterPro:IN-FAMILY:IPR011301 , InterPro:IN-FAMILY:IPR011535 , InterPro:IN-FAMILY:IPR013013 , InterPro:IN-FAMILY:IPR018113 , Pfam:IN-FAMILY:PF00367 , Pfam:IN-FAMILY:PF02378 , Prosite:IN-FAMILY:PS01035 , Prosite:IN-FAMILY:PS51098 , Prosite:IN-FAMILY:PS51103

In Paralogous Gene Group: 176 (4 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0009758 - carbohydrate utilization Inferred from experiment [Reidl91]
GO:0015768 - maltose transport Inferred from experiment [Reidl91]
GO:0046323 - glucose import Inferred from experiment [Reidl91]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0008643 - carbohydrate transport Inferred by computational analysis [UniProtGOA11a]
GO:0009401 - phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
GO:0034219 - carbohydrate transmembrane transport Inferred by computational analysis [GOA01, GOA01a]
Molecular Function: GO:0005363 - maltose transmembrane transporter activity Inferred from experiment [Reidl91]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05]
GO:0055056 - D-glucose transmembrane transporter activity Inferred from experiment [Reidl91]
GO:0008982 - protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred by computational analysis [GOA01, GOA01a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis [Reidl91]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: metabolism carbon utilization carbon compounds
transport Group Translocators Phosphotransferase Systems (PEP-dependent PTS)

Essentiality data for malX knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 28-Nov-2013 by Mackie A , Macquarie University


Enzymatic reaction of: transport of maltose (MalX PTS permease)


Enzymatic reaction of: transport of glucose (MalX PTS permease)


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 1 -> 431
[UniProt09]
UniProt: PTS EIIC type-1;
Transmembrane-Region 22 -> 42
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 69 -> 89
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 96 -> 116
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 138 -> 158
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 144
[Reidl91, UniProt10]
Alternate sequence: I → Y; UniProt: (in Ref. 1; AAA24098);
Transmembrane-Region 189 -> 209
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 289 -> 309
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 296
[Reidl91, UniProt10]
Alternate sequence: P → N; UniProt: (in Ref. 1; AAA24098);
Transmembrane-Region 321 -> 341
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 343 -> 363
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 369 -> 389
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 399 -> 419
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 432
[Reidl91, UniProt10]
Alternate sequence: E → R; UniProt: (in Ref. 1; AAA24098);
Conserved-Region 449 -> 530
[UniProt09]
UniProt: PTS EIIB type-1;
Active-Site 471
[UniProt10a]
UniProt: Phosphocysteine intermediate; for EIIB activity; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1621 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10563; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Guyer98: Guyer DM, Kao JS, Mobley HL (1998). "Genomic analysis of a pathogenicity island in uropathogenic Escherichia coli CFT073: distribution of homologous sequences among isolates from patients with pyelonephritis, cystitis, and Catheter-associated bacteriuria and from fecal samples." Infect Immun 66(9);4411-7. PMID: 9712795

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Ostblom11: Ostblom A, Adlerberth I, Wold AE, Nowrouzian FL (2011). "Pathogenicity island markers, virulence determinants malX and usp, and the capacity of Escherichia coli to persist in infants' commensal microbiotas." Appl Environ Microbiol 77(7);2303-8. PMID: 21317254

Otsuka96: Otsuka J, Watanabe H, Mori KT (1996). "Evolution of transcriptional regulation system through promiscuous coupling of regulatory proteins with operons; suggestion from protein sequence similarities in Escherichia coli." J Theor Biol 1996;178(2);183-204. PMID: 8729576

Postma93: Postma PW, Lengeler JW, Jacobson GR (1993). "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria." Microbiol Rev 57(3);543-94. PMID: 8246840

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Reidl91: Reidl J, Boos W (1991). "The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system." J Bacteriol 173(15);4862-76. PMID: 1856179

Saier14: Saier MH, Reddy VS, Tamang DG, Vastermark A (2014). "The transporter classification database." Nucleic Acids Res 42(1);D251-8. PMID: 24225317

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Lloyd08: Lloyd GS, Hollands K, Godfrey RE, Busby SJ (2008). "Transcription initiation in the Escherichia coli K-12 malI-malX intergenic region and the role of the cyclic AMP receptor protein." FEMS Microbiol Lett 288(2);250-7. PMID: 19054084

Lloyd10: Lloyd GS, Godfrey RE, Busby SJ (2010). "Targets for the MalI repressor at the divergent Escherichia coli K-12 malX-malI promoters." FEMS Microbiol Lett 305(1);28-34. PMID: 20141531

Reidl89: Reidl J, Romisch K, Ehrmann M, Boos W (1989). "MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteins GalR, CytR, and LacI." J Bacteriol 1989;171(9);4888-99. PMID: 2670898

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, BIOCYC14A.