PTS system mannitol-specific EIICBA component (P00550)

Identification
Name:PTS system mannitol-specific EIICBA component
Synonyms:
  • EIICBA-Mtl
  • EII-Mtl
  • Mannitol permease IIC component
  • PTS system mannitol-specific EIIC component
  • Mannitol-specific phosphotransferase enzyme IIB component
  • PTS system mannitol-specific EIIB component
  • Mannitol-specific phosphotransferase enzyme IIA component
  • PTS system mannitol-specific EIIA component
Gene Name:mtlA
Enzyme Class:
Biological Properties
General Function:Involved in transporter activity
Specific Function:The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannitol transport
Cellular Location:Cell inner membrane; Multi-pass membrane protein
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
KEGG Reactions:
1.0Protein N(pi)-phospho-L-histidine+1.0Thumb ↔ 1.0Protein histidine+1.0Thumb
1.0Protein N(pi)-phospho-L-histidine + 1.0Mannitol ↔ 1.0Protein histidine + 1.0Sorbitol-6-phosphate
ReactionCard
1.0Protein N(pi)-phospho-L-histidine+1.0Sugar ↔ 1.0Protein histidine+1.0Thumb
1.0Protein N(pi)-phospho-L-histidine + 1.0Sugar ↔ 1.0Protein histidine + 1.0Sugar phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0HPr - phosphorylated → 1.0Thumb+1.0HPr
1.0Mannitol + 1.0HPr - phosphorylated → 1.0Mannitol 1-phosphate + 1.0HPr
ReactionCard
1.0Diacetylchitobiose+1.0HPr - phosphorylated → 1.0Thumb+1.0HPr
1.0Diacetylchitobiose + 1.0HPr - phosphorylated → 1.0Diacetylchitobiose-6-phosphate + 1.0HPr
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0Mannitol → 1.0Sorbitol-6-phosphate + 1.0Pyruvic acid
ReactionCard
Complex Reactions:
1.0Protein EIIA N(pi)-phospho-L-histidine+1.0protein EIIB → 1.0protein EIIA+1.0protein EIIB N(pi)-phospho-L-histidine/cysteine
1.0Protein EIIA N(pi)-phospho-L-histidine + 1.0protein EIIB → 1.0protein EIIA + 1.0protein EIIB N(pi)-phospho-L-histidine/cysteine
ReactionCard
1.0Protein EIIB N(pi)-phospho-L-histidine/cysteine+1.0Thumb → 1.0protein EIIB+1.0sugar phosphate
1.0Protein EIIB N(pi)-phospho-L-histidine/cysteine + 1.0Sucrose → 1.0protein EIIB + 1.0sugar phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20547Diacetylchitobiose-6-phosphateMetaboCard
ECMDB00765MannitolMetaboCard
ECMDB21434Mannitol 1-phosphateMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01400Sorbitol-6-phosphateMetaboCard
ECMDB00258SucroseMetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane
membrane part
Function
carbohydrate transmembrane transporter activity
cation transmembrane transporter activity
cation:sugar symporter activity
ion transmembrane transporter activity
protein-N(PI)-phosphohistidine-sugar phosphotransferase activity
solute:cation symporter activity
substrate-specific transmembrane transporter activity
sugar:hydrogen symporter activity
transmembrane transporter activity
transporter activity
Process
carbohydrate transport
establishment of localization
phosphoenolpyruvate-dependent sugar phosphotransferase system
transport
Gene Properties
Blattner:b3599
Gene OrientationClockwise
Centisome Percentage:81.26
Left Sequence End3770304
Right Sequence End3772217
Gene Sequence:
>1914 bp
ATGTCATCCGATATTAAGATCAAAGTGCAAAGCTTTGGTCGTTTCCTCAGCAACATGGTG
ATGCCAAATATCGGCGCGTTTATCGCGTGGGGTATCATCACCGCGTTATTTATTCCAACA
GGGTGGTTACCGAACGAGACGCTGGCGAAGCTGGTCGGGCCGATGATCACTTATCTCCTG
CCGCTGCTGATCGGTTATACCGGTGGTAAGCTGGTAGGCGGCGAACGTGGCGGCGTAGTC
GGTGCCATCACCACCATGGGCGTTATCGTCGGCGCAGACATGCCGATGTTCCTCGGTTCT
ATGATTGCAGGTCCGCTGGGCGGCTGGTGCATTAAGCACTTCGACCGCTGGGTAGACGGT
AAGATCAAATCCGGTTTTGAGATGCTGGTGAATAACTTCTCCGCAGGCATCATCGGGATG
ATCCTCGCTATTCTGGCATTCCTCGGCATTGGCCCGATTGTTGAAGCCCTGTCCAAAATG
CTGGCTGCGGGCGTTAACTTCATGGTTGTCCATGACATGCTGCCGCTGGCGTCTATCTTT
GTTGAACCGGCGAAAATCCTGTTCCTCAACAACGCCATTAACCACGGTATCTTCTCGCCG
CTGGGTATTCAGCAGTCCCATGAACTGGGTAAATCAATCTTCTTCCTGATTGAAGCTAAC
CCAGGTCCAGGTATGGGCGTGCTGCTGGCGTACATGTTCTTTGGTCGTGGTAGCGCTAAA
CAGTCTGCGGGCGGTGCGGCAATCATCCACTTCCTGGGGGGTATCCACGAAATCTACTTC
CCGTATGTGCTGATGAATCCGCGTCTGATCCTCGCAGTCATCCTCGGCGGTATGACTGGC
GTGTTCACGCTGACTATCCTGGGCGGTGGTCTGGTTTCTCCGGCATCTCCGGGTTCTATC
CTTGCTGTACTGGCGATGACACCAAAAGGTGCTTACTTCGCTAACATCGCGGGTGTGTGT
GCGGCGATGGCTGTCTCCTTCGTTGTCTCTGCTATTTTGCTGAAAACCAGCAAAGTGAAA
GAAGAAGATGATATTGAAGCAGCAACTCGTCGTATGCAGGACATGAAAGCTGAGTCTAAA
GGCGCATCTCCGCTGTCTGCTGGCGATGTGACTAACGACCTGAGCCACGTACGTAAAATC
ATCGTTGCCTGTGACGCCGGTATGGGTTCCAGTGCGATGGGCGCAGGCGTTCTGCGTAAG
AAAATTCAGGATGCAGGTCTGTCGCAGATTTCTGTTACTAACAGCGCGATCAACAACCTG
CCGCCAGATGTGGACCTCGTCATCACTCACCGTGACCTGACCGAACGCGCTATGCGCCAG
GTTCCGCAGGCACAGCATATTTCGCTGACCAACTTCCTCGACAGCGGCCTGTACACCAGC
CTGACCGAACGTCTGGTTGCTGCCCAACGCCACACGGCAAACGAAGAGAAAGTAAAAGAC
AGCCTGAAAGACAGCTTTGACGATTCCAGTGCTAACCTGTTCAAGCTAGGCGCGGAGAAC
ATCTTCCTCGGTCGCAAAGCGGCAACCAAAGAAGAAGCGATTCGTTTTGCTGGCGAGCAG
CTGGTGAAAGGCGGTTACGTTGAGCCGGAATACGTTCAGGCGATGCTGGATCGTGAAAAA
CTGACCCCGACTTATCTGGGTGAGTCTATCGCGGTGCCACACGGTACGGTTGAAGCGAAA
GATCGCGTACTGAAAACGGGCGTCGTGTTCTGCCAGTACCCGGAAGGCGTGCGCTTCGGT
GAAGAAGAAGATGACATTGCCCGTCTGGTGATTGGTATTGCTGCCCGTAACAACGAGCAC
ATTCAGGTTATCACCAGCCTGACCAATGCACTGGATGATGAGTCCGTCATCGAGCGTCTG
GCACACACCACCAGCGTGGATGAAGTGCTGGAACTGCTGGCAGGTCGTAAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:637
Protein Molecular Weight:67972
Protein Theoretical pI:6
PDB File:1J6T
Signaling Regions:
  • None
Transmembrane Regions:
  • 25-44
  • 51-69
  • 135-154
  • 166-184
  • 274-291
  • 314-333
Protein Sequence:
>PTS system mannitol-specific EIICBA component
MSSDIKIKVQSFGRFLSNMVMPNIGAFIAWGIITALFIPTGWLPNETLAKLVGPMITYLL
PLLIGYTGGKLVGGERGGVVGAITTMGVIVGADMPMFLGSMIAGPLGGWCIKHFDRWVDG
KIKSGFEMLVNNFSAGIIGMILAILAFLGIGPIVEALSKMLAAGVNFMVVHDMLPLASIF
VEPAKILFLNNAINHGIFSPLGIQQSHELGKSIFFLIEANPGPGMGVLLAYMFFGRGSAK
QSAGGAAIIHFLGGIHEIYFPYVLMNPRLILAVILGGMTGVFTLTILGGGLVSPASPGSI
LAVLAMTPKGAYFANIAGVCAAMAVSFVVSAILLKTSKVKEEDDIEAATRRMQDMKAESK
GASPLSAGDVTNDLSHVRKIIVACDAGMGSSAMGAGVLRKKIQDAGLSQISVTNSAINNL
PPDVDLVITHRDLTERAMRQVPQAQHISLTNFLDSGLYTSLTERLVAAQRHTANEEKVKD
SLKDSFDDSSANLFKLGAENIFLGRKAATKEEAIRFAGEQLVKGGYVEPEYVQAMLDREK
LTPTYLGESIAVPHGTVEAKDRVLKTGVVFCQYPEGVRFGEEEDDIARLVIGIAARNNEH
IQVITSLTNALDDESVIERLAHTTSVDEVLELLAGRK
References
External Links:
ResourceLink
Uniprot ID:P00550
Uniprot Name:PTM3C_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676444
PDB ID:1J6T
Ecogene ID:EG10615
Ecocyc:EG10615
ColiBase:b3599
Kegg Gene:b3599
EchoBASE ID:EB0610
CCDB:PTM3C_ECOLI
BacMap:16131470
General Reference:
  • 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
  • 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
  • Davis, T., Yamada, M., Elgort, M., Saier, M. H. Jr (1988). "Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli." Mol Microbiol 2:405-412. Pubmed: 3135464
  • 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
  • Lee, C. A., Saier, M. H. Jr (1983). "Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene." J Biol Chem 258:10761-10767. Pubmed: 6309813
  • Pas, H. H., Robillard, G. T. (1988). "S-phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl." Biochemistry 27:5835-5839. Pubmed: 3142516
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620
  • Sugiyama, J. E., Mahmoodian, S., Jacobson, G. R. (1991). "Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions." Proc Natl Acad Sci U S A 88:9603-9607. Pubmed: 1946374
  • van Montfort, R. L., Pijning, T., Kalk, K. H., Hangyi, I., Kouwijzer, M. L., Robillard, G. T., Dijkstra, B. W. (1998). "The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site." Structure 6:377-388. Pubmed: 9551558