PTS system N-acetylmuramic acid-specific EIIBC component (P77272)

Identification
Name:PTS system N-acetylmuramic acid-specific EIIBC component
Synonyms:
  • EIIBC-MurNAc
  • N-acetylmuramic acid-specific phosphotransferase enzyme IIB component
  • PTS system N-acetylmuramic acid-specific EIIB component
  • N-acetylmuramic acid permease IIC component
  • PTS system N-acetylmuramic acid-specific EIIC component
Gene Name:murP
Enzyme Class:
Biological Properties
General Function:Involved in protein-N(PI)-phosphohistidine-sugar phosphotransferase 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 N-acetylmuramic acid (MurNAc) transport, yielding cytoplasmic MurNAc-6-P. Is responsible for growth on MurNAc as the sole source of carbon and energy. Is also able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably because of the 1,6- anhydro ring
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:
1.0Thumb+1.0Protein N(pi)-phospho-L-histidine ↔ 1.0Thumb+1.0Protein histidine
1.0N-Acetyl-D-muramoate + 1.0Protein N(pi)-phospho-L-histidine ↔ 1.0N-Acetylmuramic acid 6-phosphate + 1.0Protein histidine
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:
1.0HPr - phosphorylated+1.0MurNAc+1.0MurNAc → 1.0HPr+1.0Thumb
1.0HPr - phosphorylated + 1.0MurNAc + 1.0MurNAc → 1.0HPr + 1.0MurNAc-6-P
ReactionCard
1.0Erythrose+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Erythrose + 1.0Erythrose → 1.0D-Erythrose 4-phosphate + 1.0CL(17:0cycw7c/16:1(9Z)/17:0cycw7c/19:0cycv8c) + 1.0CL(17:0cycw7c/16:0/17:0cycw7c/16:1(9Z))
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0Sucrose → 1.0Pyruvic acid + 1.0Sucrose-6-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0N-Acetyl-D-muramoate → 1.0N-Acetylmuramic acid 6-phosphate + 1.0Pyruvic acid
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
ECMDB22975CL(17:0cycw7c/16:0/17:0cycw7c/16:1(9Z))MetaboCard
ECMDB22980CL(17:0cycw7c/16:1(9Z)/17:0cycw7c/19:0cycv8c)MetaboCard
ECMDB02649D-Erythrose 4-phosphateMetaboCard
ECMDB24914ErythroseMetaboCard
ECMDB24235MurNAc-6-PMetaboCard
ECMDB20176N-Acetyl-D-muramoateMetaboCard
ECMDB20177N-Acetylmuramic acid 6-phosphateMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB00258SucroseMetaboCard
ECMDB20196Sucrose-6-phosphateMetaboCard
GO Classification:
Component
cell part
membrane
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:b2429
Gene OrientationClockwise
Centisome Percentage:54.85
Left Sequence End2544695
Right Sequence End2546119
Gene Sequence:
>1425 bp
ATGAGTACTGAAATCAAAACTCAGGTCGTGGTACTTGGGGCAGGCCCCGCAGGTTACTCC
GCTGCCTTCCGTTGCGCTGATTTAGGTCTGGAAACCGTAATCGTAGAACGTTACAACACC
CTTGGCGGTGTTTGCCTGAACGTCGGCTGTATCCCTTCTAAAGCACTGCTGCACGTAGCA
AAAGTTATCGAAGAAGCCAAAGCGCTGGCTGAACACGGTATCGTCTTCGGCGAACCGAAA
ACCGATATCGACAAGATTCGTACCTGGAAAGAGAAAGTGATCAATCAGCTGACCGGTGGT
CTGGCTGGTATGGCGAAAGGCCGCAAAGTCAAAGTGGTCAACGGTCTGGGTAAATTCACC
GGGGCTAACACCCTGGAAGTTGAAGGTGAGAACGGCAAAACCGTGATCAACTTCGACAAC
GCGATCATTGCAGCGGGTTCTCGCCCGATCCAACTGCCGTTTATTCCGCATGAAGATCCG
CGTATCTGGGACTCCACTGACGCGCTGGAACTGAAAGAAGTACCAGAACGCCTGCTGGTA
ATGGGTGGCGGTATCATCGGTCTGGAAATGGGCACCGTTTACCACGCGCTGGGTTCACAG
ATTGACGTGGTTGAAATGTTCGACCAGGTTATCCCGGCAGCTGACAAAGACATCGTTAAA
GTCTTCACCAAGCGTATCAGCAAGAAATTCAACCTGATGCTGGAAACCAAAGTTACCGCC
GTTGAAGCGAAAGAAGACGGCATTTATGTGACGATGGAAGGCAAAAAAGCACCCGCTGAA
CCGCAGCGTTACGACGCCGTGCTGGTAGCGATTGGTCGTGTGCCGAACGGTAAAAACCTC
GACGCAGGCAAAGCAGGCGTGGAAGTTGACGACCGTGGTTTCATCCGCGTTGACAAACAG
CTGCGTACCAACGTACCGCACATCTTTGCTATCGGCGATATCGTCGGTCAACCGATGCTG
GCACACAAAGGTGTTCACGAAGGTCACGTTGCCGCTGAAGTTATCGCCGGTAAGAAACAC
TACTTCGATCCGAAAGTTATCCCGTCCATCGCCTATACCGAACCAGAAGTTGCATGGGTG
GGTCTGACTGAGAAAGAAGCGAAAGAGAAAGGCATCAGCTATGAAACCGCCACCTTCCCG
TGGGCTGCTTCTGGTCGTGCTATCGCTTCCGACTGCGCAGACGGTATGACCAAGCTGATT
TTCGACAAAGAATCTCACCGTGTGATCGGTGGTGCGATTGTCGGTACTAACGGCGGCGAG
CTGCTGGGTGAAATCGGCCTGGCAATCGAAATGGGTTGTGATGCTGAAGACATCGCACTG
ACCATCCACGCGCACCCGACTCTGCACGAGTCTGTGGGCCTGGCGGCAGAAGTGTTCGAA
GGTAGCATTACCGACCTGCCGAACCCGAAAGCGAAGAAGAAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:474
Protein Molecular Weight:49801
Protein Theoretical pI:8
Signaling Regions:
  • None
Transmembrane Regions:
  • 124-144
  • 158-178
  • 181-201
  • 218-238
  • 261-281
  • 302-322
  • 335-355
  • 369-389
  • 394-414
  • 441-461
Protein Sequence:
>PTS system N-acetylmuramic acid-specific EIIBC component
MAKEISSELLNTILTRVGGPGNIASCGNCMTRLRLGVHDSSLVDPNIKTLEGVKGVILTS
DQVQVVFGPGKAHRAAKAMSELLGEAPVQDAAEIAAQNKRQLKAKQTSGVQQFLAKFATI
FTPLIPGFIAAGLLLGIATLIATVMHVPADAQGTLPDALNFMKVFSKGLFTFLVILVGYN
AAQAFGGTGVNGAIIAALFLLGYNPAATTGYYAGFHDFFGLPIDPRGNIIGVLIAAWACA
RIEGMVRRFMPDDLDMLLTSLITLLITATLAYLIIMPLGGWLFEGMSWLFMHLNSNPFGC
AVLAGLFLIAVVFGVHQGFIPVYLALMDSQGFNSLFPILSMAGAGQVGAALALYWRAQPH
SALRSQVRGAIIPGLLGVGEPLIYGVTLPRMKPFVTACLGGAAGGLFIGLIAWWGLPMGL
NSAFGPSGLVALPLMTSAQGILPAMAVYAGGILVAWVCGFIFTTLFGCRNVNLD
References
External Links:
ResourceLink
Uniprot ID:P77272
Uniprot Name:PTYBC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674337
Ecogene ID:EG14163
Ecocyc:EG14163
ColiBase:b2429
Kegg Gene:b2429
EchoBASE ID:EB3915
CCDB:PTYBC_ECOLI
BacMap:16130354
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
  • Dahl, U., Jaeger, T., Nguyen, B. T., Sattler, J. M., Mayer, C. (2004). "Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid." J Bacteriol 186:2385-2392. Pubmed: 15060041
  • 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
  • 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
  • Jaeger, T., Mayer, C. (2008). "The transcriptional factors MurR and catabolite activator protein regulate N-acetylmuramic acid catabolism in Escherichia coli." J Bacteriol 190:6598-6608. Pubmed: 18723630
  • Uehara, T., Suefuji, K., Jaeger, T., Mayer, C., Park, J. T. (2006). "MurQ Etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall." J Bacteriol 188:1660-1662. Pubmed: 16452451
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837