Difference between revisions of "SpsA"
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37910&redirect=T BSU37910] | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37910&redirect=T BSU37910] | ||
− | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1QGS 1QGS] (complex with UDP) | + | * '''Structure:''' |
+ | ** [http://www.rcsb.org/pdb/explore.do?structureId=1QGS 1QGS] (complex with UDP) {{PubMed|10350455}} | ||
+ | ** [http://www.rcsb.org/pdb/explore.do?structureId=1H7Q 1H7Q] {{PubMed|11733986}} | ||
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39621 P39621] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P39621 P39621] | ||
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=References= | =References= | ||
− | <pubmed>9353933 15383836 </pubmed> | + | <pubmed>9353933 15383836 11733986 10350455 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:49, 23 September 2014
- Description: nucleotide-sugar-dependent glycosyltransferase, spore coat polysaccharide synthesis
Gene name | spsA |
Synonyms | ipa-63d |
Essential | no |
Product | nucleotide-sugar-dependent glycosyltransferase |
Function | spore coat polysaccharide synthesis |
Gene expression levels in SubtiExpress: spsA | |
MW, pI | 30 kDa, 5.358 |
Gene length, protein length | 768 bp, 256 aa |
Immediate neighbours | spsB, gerQ |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU37910
Phenotypes of a mutant
Database entries
- BsubCyc: BSU37910
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: glycosyltransferase 2 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU37910
- UniProt: P39621
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and 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
Patrick Eichenberger, Masaya Fujita, Shane T Jensen, Erin M Conlon, David Z Rudner, Stephanie T Wang, Caitlin Ferguson, Koki Haga, Tsutomu Sato, Jun S Liu, Richard Losick
The program of gene transcription for a single differentiating cell type during sporulation in Bacillus subtilis.
PLoS Biol: 2004, 2(10);e328
[PubMed:15383836]
[WorldCat.org]
[DOI]
(I p)
N Tarbouriech, S J Charnock, G J Davies
Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases.
J Mol Biol: 2001, 314(4);655-61
[PubMed:11733986]
[WorldCat.org]
[DOI]
(P p)
S J Charnock, G J Davies
Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms.
Biochemistry: 1999, 38(20);6380-5
[PubMed:10350455]
[WorldCat.org]
[DOI]
(P p)
E Presecan, I Moszer, L Boursier, H Cruz Ramos, V de la Fuente, M-F Hullo, C Lelong, S Schleich, A Sekowska, B H Song, G Villani, F Kunst, A Danchin, P Glaser
The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees).
Microbiology (Reading): 1997, 143 ( Pt 10);3313-3328
[PubMed:9353933]
[WorldCat.org]
[DOI]
(P p)