Difference between revisions of "NagP"
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|style="background:#ABCDEF;" align="center"|'''Function''' || N-acetylglucosamine uptake and phosphorylation | |style="background:#ABCDEF;" align="center"|'''Function''' || N-acetylglucosamine uptake and phosphorylation | ||
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbohydrate_metabolic_pathways.html Sugar catabolism]''' | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 48 kDa, 7.127 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 48 kDa, 7.127 |
Revision as of 12:02, 11 June 2009
- Description: N-acetylglucosamine-specific phosphotransferase system, EIICB
Gene name | nagP |
Synonyms | yflF |
Essential | no |
Product | N-acetylglucosamine-specific phosphotransferase system, EIICB |
Function | N-acetylglucosamine uptake and phosphorylation |
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
MW, pI | 48 kDa, 7.127 |
Gene length, protein length | 1356 bp, 452 aa |
Immediate neighbours | yflG, ltaS |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU07700
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate (according to Swiss-Prot)
- Protein family: PTS permease, glucose permease (Glc) family PubMed
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot), membrane associated PubMed
Database entries
- Structure:
- Swiss prot entry: O34521
- KEGG entry: [2]
- E.C. number: 2.7.1.69
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040]
[WorldCat.org]
[DOI]
(P p)
H L Mobley, R J Doyle, U N Streips, S O Langemeier
Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis.
J Bacteriol: 1982, 150(1);8-15
[PubMed:6174502]
[WorldCat.org]
[DOI]
(P p)
- Reizer et al. (1999) Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis. Microbiology 145: 3419-3429 PubMed
- Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
- Reizer, J., Bachem, S., Reizer, A., Arnaud, M., Saier Jr., M. H. & Stülke, J. (1999) Novel phosphotransferase system genes revealed by genome analysis – the complete complement of PTS proteins encoded within the genome of Bacillus subtilis. Microbiology 145: 3419-3429. PubMed
- Mobley HL, Doyle RJ, Streips UN, Langemeier SO. (1982) Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis. J Bacteriol. Apr;150(1): 8-15. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed