P0ABG0 (PGSA_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase EC=2.7.8.5 Alternative name(s): Phosphatidylglycerophosphate synthase Short name=PGP synthase | ||||
| 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 | 182 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This protein catalyzes the committed step to the synthesis of the acidic phospholipids By similarity. HAMAP MF_01437 |
| Catalytic activity | CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate. HAMAP MF_01437 |
| Pathway | Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2. HAMAP MF_01437 |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_01437. |
| Sequence similarities | Belongs to the CDP-alcohol phosphatidyltransferase class-I family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phospholipid biosynthesis |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase 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 – 182 | 181 | CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase HAMAP MF_01437 | PRO_0000056774 | |||||
Regions | |||||||||
| Topological domain | 2 – 13 | 12 | Cytoplasmic Potential | ||||||
| Transmembrane | 14 – 38 | 25 | Helical; Potential | ||||||
| Topological domain | 39 – 61 | 23 | Periplasmic Potential | ||||||
| Transmembrane | 62 – 82 | 21 | Helical; Potential | ||||||
| Topological domain | 83 – 87 | 5 | Cytoplasmic Potential | ||||||
| Transmembrane | 88 – 108 | 21 | Helical; Potential | ||||||
| Topological domain | 109 – 146 | 38 | Periplasmic Potential | ||||||
| Transmembrane | 147 – 169 | 23 | Helical; Potential | ||||||
| Topological domain | 170 – 182 | 13 | Cytoplasmic 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 | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG56927.1. BA000007 Genomic DNA. Translation: BAB36073.1. |
| PIR | B90960. C85808. |
| RefSeq | NP_288373.1. NC_002655.2. NP_310677.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P0ABG0. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000026635; EBESCP00000025528; EBESCG00000025688. EBESCT00000058874; EBESCP00000056702; EBESCG00000057922. |
| GeneID | 913922. 961910. |
| GenomeReviews | Gene locus Z3000 in contig AE005174_GR. Gene locus ECs2650 in contig BA000007_GR. |
| KEGG | ece:Z3000. ecs:ECs2650. |
| PATRIC | 18354682. VBIEscCol44059_2549. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009502. |
| HOGENOM | HBG686655. |
| OMA | WSYMAAS. |
| ProtClustDB | PRK10832. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS2650-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01437. PgsA. [Tree] |
| InterPro | IPR000462. CDP-OH_P_trans. IPR023762. PGP_synthase_bac. IPR004570. Phosphatidylglycerol_P_synth. [Graphical view] |
| KO | K00995. |
| Pfam | PF01066. CDP-OH_P_transf. 1 hit. [Graphical view] |
| PIRSF | PIRSF000847. Phos_ph_gly_syn. 1 hit. |
| TIGRFAMs | TIGR00560. PgsA. 1 hit. |
| PROSITE | PS00379. CDP_ALCOHOL_P_TRANSF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PGSA_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0ABG0 Secondary accession number(s): P06978 | ||||||||
| 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 |

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