P56527 (APHA_PROMI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 60.
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: Class B acid phosphatase Short name=CBAP 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)
| Function | Dephosphorylates several organic phosphate monoesters. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds By similarity. |
| 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 By similarity. |
| 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 metal 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 | |||||
Regions | |||||||||
| Region | 137 – 138 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 69 | 1 | Nucleophile By similarity | ||||||
| Active site | 71 | 1 | Proton donor By similarity | ||||||
| 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, CONCEPTUAL TRANSLATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M11587 Genomic DNA. No translation available. |
3D structure databases | |
| ProteinModelPortal | P56527. |
| SMR | P56527. Positions 31-160. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.50.1000. 1 hit. |
| InterPro | IPR005519. Acid_phosphat_B. IPR023214. HAD-like_dom. IPR010025. HAD-SF_ppase_IIIB_AphA. [Graphical view] |
| Pfam | PF03767. Acid_phosphat_B. 1 hit. [Graphical view] |
| SUPFAM | SSF56784. HAD-like_dom. 1 hit. |
| 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 program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
