U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

phoA alkaline phosphatase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945041, updated on 3-Dec-2024

Summary

Go to the top of the page Help
Official Symbol
phoA
Official Full Name
alkaline phosphatase
Primary source
ECOCYC:EG10727
Locus tag
b0383
See related
ASAP:ABE-0001328
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0378; psiA
Summary
Arg22 is removed from the mature enzyme by Iap to form isozyme 3. [More information is available at EcoGene: EG10727]. Alkaline phosphatase is a dimer that occurs in three forms, depending upon the growth conditions of the cell. [More information is available at EcoCyc: EG10727].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Sequence:
NC_000913.3 (401747..403162)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene D-alanine--D-alanine ligase A Neighboring gene anti-adaptor protein IraP Neighboring gene phosphate starvation-inducible protein PsiF Neighboring gene diguanylate cyclase DgcC

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes. Holtz KM, et al. Protein Sci, 2000 May. PMID 10850800, Free PMC Article
  2. Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites. Ma L, et al. Protein Sci, 1995 Aug. PMID 8520475, Free PMC Article
  3. Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites. Ma L, et al. Biochemistry, 1996 Feb 20. PMID 8652582
  4. 3-D structure of the D153G mutant of Escherichia coli alkaline phosphatase: an enzyme with weaker magnesium binding and increased catalytic activity. Dealwis CG, et al. Protein Eng, 1995 Sep. PMID 8746724
  5. Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphatase provides the secretion efficiency and is involved in the interaction with anionic phospholipids. Nesmeyanova MA, et al. FEBS Lett, 1997 Feb 17. PMID 9042967

See all (112) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.
    Title: Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.
  2. Results support a model in which the Arg166 contributes to enzymatic phosphoryl transfer through binding interactions and through additional transition state stabilization.
    Title: Arginine coordination in enzymatic phosphoryl transfer: evaluation of the effect of Arg166 mutations in Escherichia coli alkaline phosphatase.
  3. RpoS contributes to the repression of alkaline phosphatase under excess of Phosphorus.
    Title: Alkaline phosphatase as a reporter of sigma(S) levels and rpoS polymorphisms in different E. coli strains.
  4. Data report the identification of a unique slipknot feature in the fold of a well-known thermostable protein, alkaline phosphatase (phoA).
    Title: Identification of rare slipknots in proteins and their implications for stability and folding.
  5. N-terminus verified by Edman degradation on mature peptide
    Title: Amino acid sequence of Escherichia coli alkaline phosphatase.
  6. the S102T mutation resulted in a shift in the rate-determining step in the mechanism allowing us to trap the covalent intermediate of the reaction in the crystal
    Title: Trapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine.
  7. differences in metal binding between bovine and Escherichia coli alkaline phosphatases
    Title: Distinct structure and activity recoveries reveal differences in metal binding between mammalian and Escherichia coli alkaline phosphatases.
  8. The structural and functional data together suggest that some of these distinct functional groups provide specific substrate binding interactions, whereas others tune active site itself to discriminate between phosphate diester and monoester substrates.
    Title: Structural and functional comparisons of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implications for mechanism and evolution.
  9. unfolded PhoA is targeted to the TatBC translocon of Escherichia coli
    Title: Targeting of unfolded PhoA to the TAT translocon of Escherichia coli.
Submit: New GeneRIF Correction

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables alkaline phosphatase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables alkaline phosphatase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables alkaline phosphatase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrogenase (acceptor) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables magnesium ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity, acting on phosphorus or arsenic in donors IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphatase activity IEA
Inferred from Electronic Annotation
more info
  
enables phosphoprotein phosphatase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in protein dephosphorylation IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in periplasmic space IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
  

General protein information

Go to the top of the page Help
Preferred Names
alkaline phosphatase
NP_414917.2

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    401747..403162
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414917.2 alkaline phosphatase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_414917.2

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A775THJ3, A0A8I0CHG6
    Conserved Domains (1) summary
    PRK10518
    Location:1 → 471
    PRK10518; alkaline phosphatase; Provisional
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.