Reviewed,
UniProtKB/Swiss-Prot Q8X5L7 (BCSA_ECO57)
Last modified
June 16, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cellulose synthase catalytic subunit [UDP-forming] EC=2.4.1.12 | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 872 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cellulose and thin aggregative fimbriae leads to a hydrophobic network with tightly packed cells embedded in a highly inert matrix By similarity. |
| Catalytic activity | UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1). |
| Cofactor | Magnesium By similarity. |
| Enzyme regulation | Activated by bis-(3'-5') cyclic diguanylic acid (c-di-GMP) By similarity. |
| Pathway | |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein Potential. |
| Domain | There are two conserved domains in the globular part of the protein: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site. |
| Sequence similarities | Belongs to the glycosyltransferase 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cellulose biosynthesis |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Transmembrane |
| Ligand | c-di-GMP |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | UDP-glucose metabolic process Inferred from electronic annotation. Source: InterPro cellulose biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to plasma membrane Inferred from electronic annotation. Source: InterPro |
| Molecular function | cellulose synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 872 | 872 | Cellulose synthase catalytic subunit [UDP-forming] | PRO_0000059268 | |||||
Regions | |||||||||
| Transmembrane | 30 – 50 | 21 | Potential | ||||||
| Transmembrane | 151 – 171 | 21 | Potential | ||||||
| Transmembrane | 173 – 193 | 21 | Potential | ||||||
| Transmembrane | 230 – 250 | 21 | Potential | ||||||
| Transmembrane | 525 – 545 | 21 | Potential | ||||||
| Transmembrane | 547 – 567 | 21 | Potential | ||||||
| Transmembrane | 592 – 612 | 21 | Potential | ||||||
| Transmembrane | 640 – 660 | 21 | Potential | ||||||
| Transmembrane | 668 – 688 | 21 | Potential | ||||||
| Transmembrane | 833 – 853 | 21 | Potential | ||||||
| Region | 271 – 364 | 94 | Catalytic subdomain A | ||||||
| Region | 441 – 501 | 61 | Catalytic subdomain B | ||||||
Sites | |||||||||
| Active site | 313 | 1 | Potential | ||||||
| Active site | 457 | 1 | Potential | ||||||
| Binding site | 360 | 1 | Substrate Potential | ||||||
| Binding site | 362 | 1 | Substrate Potential | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG58675.1. Different initiation. BA000007 Genomic DNA. Translation: BAB37836.1. Different initiation. | |
| PIR | E91180. G86026. |
| RefSeq | NP_290113.2. NP_312440.2. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 915726. 961086. |
| GenomeReviews | Gene locus Z4948 in contig AE005174_GR. Gene locus ECs4413 in contig BA000007_GR. |
| KEGG | ece:Z4948. ecs:ECs4413. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8X5L7. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS4413-MON. |
Family and domain databases | |
| InterPro | IPR003919. Cell_synth_A. IPR017480. Cellulose_synth_catalytic. IPR001173. Glyco_trans_2. IPR009875. PilZ. [Graphical view] |
| Pfam | PF00535. Glycos_transf_2. 1 hit. PF07238. PilZ. 1 hit. [Graphical view] |
| PRINTS | PR01439. CELLSNTHASEA. |
| TIGRFAMs | TIGR03030. CelA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | BCSA_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8X5L7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


