Maltose transport system permease protein malF (P02916)

Identification
Name:Maltose transport system permease protein malF
Synonyms:Not Available
Gene Name:malF
Enzyme Class:Not Available
Biological Properties
General Function:Involved in transporter activity
Specific Function:Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane
Cellular Location:Cell inner membrane; Multi-pass membrane protein; Periplasmic side.
SMPDB Pathways:
KEGG Pathways:
Transports:
Transport References:
  • Uniprot Consortium (2012). "Reorganizing the protein space at the Universal Protein Resource (UniProt)." Nucleic Acids Res 40:D71-D75. Pubmed: 22102590
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Adenosine diphosphate+1.0Thumb
1.0Maltotetraose + 1.0Adenosine triphosphate + 1.0Water → 1.0Maltotetraose + 1.0Phosphate + 1.0Hydrogen ion + 1.0Adenosine diphosphate + 1.0ADP
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Maltotriose + 1.0Adenosine triphosphate + 1.0Water → 1.0Adenosine diphosphate + 1.0Phosphate + 1.0Hydrogen ion + 1.0Maltotriose + 1.0ADP
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Adenosine diphosphate+1.0Thumb
1.0D-Maltose + 1.0Adenosine triphosphate + 1.0Water → 1.0D-Maltose + 1.0Phosphate + 1.0Hydrogen ion + 1.0Adenosine diphosphate + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0D-Maltose → 1.0ADP + 1.0Hydrogen ion + 1.0D-Maltose + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Maltotriose → 1.0ADP + 1.0Hydrogen ion + 1.0Maltotriose + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Maltotetraose → 1.0ADP + 1.0Hydrogen ion + 1.0Maltotetraose + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.01,4-alpha-D-glucan → 1.01,4-alpha-D-glucan + 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Maltohexaose → 1.0ADP + 1.0Hydrogen ion + 1.0Maltohexaose + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Maltopentaose → 1.0ADP + 1.0Hydrogen ion + 1.0Maltopentaose + 1.0Phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211101,4-alpha-D-glucanMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00163D-MaltoseMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21243MaltohexaoseMetaboCard
ECMDB21244MaltopentaoseMetaboCard
ECMDB01296MaltotetraoseMetaboCard
ECMDB01262MaltotrioseMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
membrane
Function
transporter activity
Process
establishment of localization
transport
Gene Properties
Blattner:b4033
Gene OrientationCounterclockwise
Centisome Percentage:91.42
Left Sequence End4241554
Right Sequence End4243098
Gene Sequence:
>1545 bp
ATGTGGGATGTCATTGATTTATCGCGCTGGCAGTTTGCTCTGACCGCGCTGTATCACTTT
TTATTTGTACCCCTTACCCTGGGGCTGATTTTTTTGCTGGCTATTATGGAAACCATTTAC
GTGGTCACCGGCAAAACAATCTACCGCGATATGACGCGCTTCTGGGGTAAGCTCTTCGGT
ATCAATTTTGCTCTTGGCGTGGCTACCGGCCTGACCATGGAGTTTCAGTTTGGTACTAAC
TGGTCATTCTATTCCAACTATGTGGGCGATATTTTTGGCGCACCGCTGGCGATGGAAGCA
TTAATGGCCTTCTTCCTCGAATCCACCTTTGTCGGGCTGTTCTTCTTCGGCTGGCAACGG
CTGAATAAATACCAGCACCTGCTGGTGACGTGGCTGGTGGCGTTCGGTTCAAATCTCTCT
GCGTTGTGGATATTGAATGCCAACGGTTGGATGCAATACCCGACCGGTGCGCATTTTGAT
ATCGACACCCTGCGTATGGAGATGACCAGCTTCAGCGAGCTGGTCTTTAATCCGGTCAGC
CAGGTGAAATTTGTGCACACCGTAATGGCGGGCTACGTGACCGGGGCCATGTTTATTATG
GCGATCAGCGCCTGGTATTTACTGCGCGGACGGGAGCGCAATGTCGCATTACGCTCGTTT
GCCATCGGTTCCGTCTTCGGTACTCTGGCGATTATCGGTACCCTGCAACTCGGAGACAGT
TCTGCGTATGAAGTCGCGCAAGTACAACCGGTAAAACTGGCGGCGATGGAAGGGGAGTGG
CAAACGGAACCTGCACCTGCACCGTTCCATGTGGTTGCCTGGCCGGAACAGGATCAAGAG
CGTAACGCCTTTGCCCTCAAAATTCCCGCGCTGCTAGGGATCCTCGCCACTCACTCATTA
GATAAACCCGTGCCGGGTCTGAAGAATTTGATGGCTGAAACCTACCCACGCTTGCAACGC
GGACGTATGGCCTGGCTGTTAATGCAGGAAATATCGCAAGGCAATCGTGAGCCGCATGTG
TTGCAGGCATTCCGGGGACTGGAAGGTGACCTGGGCTACGGCATGTTGCTCTCCCGCTAT
GCGCCGGATATGAATCATGTCACAGCCGCACAGTACCAGGCGGCGATGCGTGGCGCGATA
CCTCAGGTTGCGCCGGTATTCTGGAGTTTCCGCATCATGGTGGGCTGTGGTTCCCTGCTG
CTACTGGTGATGCTGATTGCGCTTGTCCAGACGCTGCGTGGCAAAATCGACCAGCATCGC
TGGGTGCTGAAAATGGCGCTCTGGAGTTTGCCGTTGCCGTGGATTGCGATTGAAGCCGGG
TGGTTTATGACCGAGTTTGGTCGTCAGCCGTGGGCGATACAGGACATCTTACCGACATAC
TCCGCGCACTCCGCTTTAACCACAGGACAACTGGCTTTCTCACTGATCATGATCGTAGGG
CTTTACACCCTGTTCTTAATCGCCGAAGTCTACCTGATGCAGAAATATGCCCGTCTGGGG
CCGAGCGCGATGCAGAGTGAACAACCGACGCAGCAACAGGGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:514
Protein Molecular Weight:57013
Protein Theoretical pI:9
Signaling Regions:
  • None
Transmembrane Regions:
  • 17-36
  • 40-58
  • 67-92
  • 276-306
  • 319-336
  • 370-392
  • 426-452
  • 484-505
Protein Sequence:
>Maltose transport system permease protein malF
MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANR
KAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTY
NFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNR
QALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSI
TADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGM
VLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPA
WFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLP
LLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGG
GQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD
References
External Links:
ResourceLink
Uniprot ID:P02916
Uniprot Name:MALF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651479
Ecogene ID:EG10555
Ecocyc:EG10555
ColiBase:b4033
Kegg Gene:b4033
EchoBASE ID:EB0550
CCDB:MALF_ECOLI
BacMap:16131859
General Reference:
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Boos, W., Shuman, H. (1998). "Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation." Microbiol Mol Biol Rev 62:204-229. Pubmed: 9529892
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Dassa, E., Hofnung, M. (1985). "Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems." EMBO J 4:2287-2293. Pubmed: 3000770
  • Ehrle, R., Pick, C., Ulrich, R., Hofmann, E., Ehrmann, M. (1996). "Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis." J Bacteriol 178:2255-2262. Pubmed: 8636026
  • Ehrmann, M., Boyd, D., Beckwith, J. (1990). "Genetic analysis of membrane protein topology by a sandwich gene fusion approach." Proc Natl Acad Sci U S A 87:7574-7578. Pubmed: 2170984
  • Froshauer, S., Beckwith, J. (1984). "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." J Biol Chem 259:10896-10903. Pubmed: 6088520
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Heijne, G. (1986). "The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology." EMBO J 5:3021-3027. Pubmed: 16453726
  • Hunke, S., Mourez, M., Jehanno, M., Dassa, E., Schneider, E. (2000). "ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking." J Biol Chem 275:15526-15534. Pubmed: 10809785
  • McGovern, K., Ehrmann, M., Beckwith, J. (1991). "Decoding signals for membrane protein assembly using alkaline phosphatase fusions." EMBO J 10:2773-2782. Pubmed: 1915262
  • Merino, G., Shuman, H. A. (1997). "Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system." J Bacteriol 179:7687-7694. Pubmed: 9401026
  • Mourez, M., Hofnung, M., Dassa, E. (1997). "Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits." EMBO J 16:3066-3077. Pubmed: 9214624