P58130 (PLSB_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glycerol-3-phosphate acyltransferase Short name=GPAT EC=2.3.1.15 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 807 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. HAMAP MF_00393 |
| Pathway | Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393 |
| Subcellular location | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_00393. |
| Domain | The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity. HAMAP MF_00393 |
| Sequence similarities | Belongs to the GPAT/DAPAT family. |
| Sequence caution | The sequence AAG59240.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB38447.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phospholipid biosynthesis |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | glycerol-3-phosphate O-acyltransferase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 807 | 806 | Glycerol-3-phosphate acyltransferase HAMAP MF_00393 | PRO_0000195220 | |||||
Regions | |||||||||
| Motif | 306 – 311 | 6 | HXXXXD motif HAMAP MF_00393 | ||||||
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 | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG59240.1. Different initiation. BA000007 Genomic DNA. Translation: BAB38447.1. Different initiation. |
| PIR | D86097. H91256. |
| RefSeq | NP_290675.2. NC_002655.2. NP_313051.2. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P58130. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000026259; EBESCP00000025152; EBESCG00000025312. EBESCT00000057388; EBESCP00000055216; EBESCG00000056436. |
| GeneID | 915055. 960082. |
| GenomeReviews | Gene locus Z5640 in contig AE005174_GR. Gene locus ECs5024 in contig BA000007_GR. |
| KEGG | ece:Z5640. ecs:ECs5024. |
| PATRIC | 18359643. VBIEscCol44059_4958. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000010697. |
| HOGENOM | HBG296590. |
| OMA | WNKLYQG. |
| ProtClustDB | PRK04974. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS5024-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00393. Glyc3P_acyltrans. [Tree] |
| InterPro | IPR002123. Acyltransferase. IPR022284. G3P_O-AcylTrfase. [Graphical view] |
| KO | K00631. |
| Pfam | PF01553. Acyltransferase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000437. GPAT_DHAPAT. 1 hit. |
| SMART | SM00563. PlsC. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03703. PlsB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PLSB_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P58130 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with