Reviewed,
UniProtKB/Swiss-Prot P56527 (APHA_PROMI)
Last modified
June 16, 2009.
Version 47.
History...
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90%,
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Class B acid phosphatase EC=3.1.3.2 | ||||
| Gene names |
| ||||
| Organism | Proteus mirabilis | ||||
| Taxonomic identifier | 584 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus |
Protein attributes
| Sequence length | 160 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | A phosphate monoester + H2O = an alcohol + phosphate. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Periplasm Potential. |
| Sequence similarities | Belongs to the class B bacterial acid phosphatase family. |
| Sequence caution | The sequence M11587 differs from that shown. Reason: Frameshift at several positions. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| Gene Ontology (GO) | |
| Cellular component | outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro |
| Molecular function | acid phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | By similarity | ||||||
| Chain | 24 – ›160 | ›137 | Class B acid phosphatase | PRO_0000024007 | |||||
Sites | |||||||||
| Metal binding | 69 | 1 | Magnesium By similarity | ||||||
| Metal binding | 71 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 160 | 1 | |||||||
Sequences
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References
| [1] | "Nucleotide sequence analysis of the cat gene of Proteus mirabilis: comparison with the type I (Tn9) cat gene." Charles I.G., Keyte J.W., Shaw W.V. J. Bacteriol. 164:123-129(1985) [PubMed: 3900035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Cloning and characterization of the NapA acid phosphatase/phosphotransferase of Morganella morganii: identification of a new family of bacterial acid-phosphatase-encoding genes." Thaller M.C., Lombardi G., Berlutti F., Schippa S., Rossolini G.M. Microbiology 141:147-154(1995) [PubMed: 7894706] [Abstract] Cited for: IDENTIFICATION, CONCEPTUAL TRANSLATION. |
Cross-references
Sequence databases | |
|---|---|
| M11587 Genomic DNA. No translation available. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.2. 639. |
Family and domain databases | |
| InterPro | IPR005519. Acid_phosphat_B. IPR010025. HAD-SF_ppase_IIIB_AphA. [Graphical view] |
| Pfam | PF03767. Acid_phosphat_B. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01672. AphA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | APHA_PROMI | ||||||||
| Accession | Primary (citable) accession number: P56527 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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