Q5HED0 (ACPS_STAAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 50.
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: Holo-[acyl-carrier-protein] synthase Short name=Holo-ACP synthase EC=2.7.8.7 Alternative name(s): 4'-phosphopantetheinyl transferase AcpS | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain COL) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 93062 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 119 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein By similarity. HAMAP MF_00101 |
| Catalytic activity | CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]. HAMAP MF_00101 |
| Cofactor | Magnesium By similarity. HAMAP MF_00101 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00101. |
| Sequence similarities | Belongs to the P-Pant transferase superfamily. AcpS family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Transferase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW macromolecule biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | holo-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 119 | 119 | Holo-[acyl-carrier-protein] synthase HAMAP MF_00101 | PRO_0000175700 | |||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||
| Metal binding | 8 | 1 | Magnesium By similarity | ||||||||||||||||||||||||||||
| Metal binding | 59 | 1 | Magnesium By similarity | ||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Beta strand | 8 – 11 | 4 | |||||||||||||||||||||||||||||
| Helix | 12 – 20 | 9 | |||||||||||||||||||||||||||||
| Helix | 23 – 25 | 3 | |||||||||||||||||||||||||||||
| Helix | 26 – 29 | 4 | |||||||||||||||||||||||||||||
| Helix | 32 – 39 | 8 | |||||||||||||||||||||||||||||
| Helix | 44 – 51 | 8 | |||||||||||||||||||||||||||||
| Helix | 55 – 64 | 10 | |||||||||||||||||||||||||||||
| Helix | 75 – 77 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 80 – 82 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 88 – 90 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 96 – 103 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 105 – 115 | 11 | |||||||||||||||||||||||||||||
Sequences
References
| [1] | "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. Fraser C.M.J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: COL. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | CP000046 Genomic DNA. Translation: AAW37023.1. | ||||||||||||
| RefSeq | YP_186877.1. NC_002951.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q5HED0. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | Q5HED0. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBSTAT00000009170; EBSTAP00000008905; EBSTAG00000009169. | ||||||||||||
| GeneID | 3238092. | ||||||||||||
| GenomeReviews | Gene locus SACOL2061 in contig CP000046_GR. | ||||||||||||
| KEGG | sac:SACOL2061. | ||||||||||||
| PATRIC | 19530397. VBIStaAur112458_2010. | ||||||||||||
| TIGR | SACOL2061. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0736. | ||||||||||||
| GeneTree | EBGT00050000025046. | ||||||||||||
| HOGENOM | HBG734479. | ||||||||||||
| OMA | VHVSITH. | ||||||||||||
| ProtClustDB | PRK00070. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | SAUR93062:SACOL2061-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00101. AcpS. [Tree] | ||||||||||||
| InterPro | IPR008278. 4-PPantetheinyl_Trfase. IPR002582. ACPS. IPR004568. PPantethiene-prot_Trfase. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.90.470.20. G3DSA:3.90.470.20. 1 hit. | ||||||||||||
| KO | K00997. | ||||||||||||
| Pfam | PF01648. ACPS. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD004282. PPantethiene-prot_Trfase. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| SUPFAM | SSF56214. 4-PPT_transf. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00516. AcpS. 1 hit. TIGR00556. Pantethn_trn. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | ACPS_STAAC | ||||||||
| Accession | Primary (citable) accession number: Q5HED0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with