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P56527 (APHA_PROMI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Class B acid phosphatase

Short name=CBAP
EC=3.1.3.2
Gene names
Name:aphA
Synonyms:napA
OrganismProteus mirabilis
Taxonomic identifier584 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length160 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 componentPeriplasm
   DomainSignal
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
Gene Ontology (GO)
   Cellular_componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionacid phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 By similarity
Chain24 – ›160›137Class B acid phosphatase
PRO_0000024007

Regions

Region137 – 1382Substrate binding By similarity

Sites

Active site691Nucleophile By similarity
Active site711Proton donor By similarity
Metal binding691Magnesium By similarity
Metal binding711Magnesium; via carbonyl oxygen By similarity

Experimental info

Non-terminal residue1601

Sequences

Sequence LengthMass (Da)Tools
P56527 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 395541C45A456735

FASTA16018,081
        10         20         30         40         50         60 
MRKVTLTLSA IALALSLNGA AMAKVHMPEV VSQGVTVTEL AHQQPIKWVS VAEIEKSLEG 

        70         80         90        100        110        120 
QAPMAVGFDI DDTFWFSSPG FYRVKLEYSP NDFSYLKNPE FWEKMNNEWD KFSMPKQVGI 

       130        140        150        160 
DLVQMHLKRG DTVYFITGRT QTKTETCVTK YVQEGLNIPA 

« Hide

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

ProteinModelPortalP56527.
SMRP56527. Positions 31-160.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]
PfamPF03767. Acid_phosphat_B. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01672. AphA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPHA_PROMI
AccessionPrimary (citable) accession number: P56527
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families