RegulonDB RegulonDB 11.1: Gene Form
   

phoA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

phoA psiF iraP PhoB terminator anti-terminator psiFp psiFp phoAp phoAp TSS_495 TSS_495

Gene      
Name: phoA    Texpresso search in the literature
Synonym(s): ECK0378, EG10727, b0383, psiA
Genome position(nucleotides): 401747 --> 403162
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 53.39
Reference(s): [1] Kikuchi Y., et al., 1981
External database links:  
ASAP:
 ABE-0001328
CGSC:
 398
ECHOBASE:
 EB0720
ECOLIHUB:
 phoA
OU-MICROARRAY:
 b0383
STRING:
 511145.b0383
COLOMBOS: phoA


Product      
Name: alkaline phosphatase
Synonym(s): PhoA, PsiA
Sequence: Get amino acid sequence Fasta Format
Cellular location: periplasmic space
Molecular weight: 49.439
Isoelectric point: 6.02
Motif(s):
 
Type Positions Sequence Comment
1 -> 21 MKQSTIALALLPLLFTPVTKA
10 -> 10 L UniProt: In Ref. 12; AAA23431..
22 -> 22 R UniProt: In isozyme 3..
64 -> 431 AKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDS
78 -> 80 SEI UniProt: In Ref. 8; AAA24359..

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.8 - metabolism of other compounds --> 1.8.1 - phosphorous metabolism
Gene Ontology Terms (GO)  
cellular_component GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space
molecular_function GO:0003824 - catalytic activity
GO:0005515 - protein binding
GO:0016787 - hydrolase activity
GO:0046872 - metal ion binding
GO:0004721 - phosphoprotein phosphatase activity
GO:0016791 - phosphatase activity
GO:0008270 - zinc ion binding
GO:0004035 - alkaline phosphatase activity
GO:0030613 - oxidoreductase activity, acting on phosphorus or arsenic in donors
GO:0000287 - magnesium ion binding
GO:0033748 - hydrogenase (acceptor) activity
biological_process GO:0006470 - protein dephosphorylation
GO:0016311 - dephosphorylation
Note(s): Note(s): ...[more].
Reference(s): [2] Applebury ML., et al., 1970
[3] Ghosh AK., et al., 2021
[4] Horiuchi T., et al., 1959
[5] Inouye H., et al., 1977
[6] Le Du MH., et al., 2002
[7] Ma L., et al., 1996
[8] Ma L., et al., 1995
[9] Michaelis S., et al., 1983
[10] Nesmeyanova MA., et al., 1981
[11] Schlesinger MJ. 1968
[12] Torriani A. 1968
External database links:  
ALPHAFOLD:
 P00634
DIP:
 DIP-10496N
ECOCYC:
 ALKAPHOSPHA-MONOMER
ECOLIWIKI:
 b0383
INTERPRO:
 IPR018299
INTERPRO:
 IPR001952
INTERPRO:
 IPR017850
MODBASE:
 P00634
PANTHER:
 PTHR11596
PDB:
 1AJA
PDB:
 1AJB
PDB:
 1AJC
PDB:
 1AJD
PDB:
 1ALH
PDB:
 1ALI
PDB:
 1ALJ
PDB:
 1ALK
PDB:
 1ANI
PDB:
 1ANJ
PDB:
 1B8J
PDB:
 1ED8
PDB:
 1ED9
PDB:
 1ELX
PDB:
 1ELY
PDB:
 1ELZ
PDB:
 1EW8
PDB:
 1EW9
PDB:
 1HJK
PDB:
 1HQA
PDB:
 1KH4
PDB:
 1KH5
PDB:
 1KH7
PDB:
 1KH9
PDB:
 1KHJ
PDB:
 1KHK
PDB:
 1KHL
PDB:
 1KHN
PDB:
 1URA
PDB:
 1URB
PDB:
 1Y6V
PDB:
 1Y7A
PDB:
 2ANH
PDB:
 2G9Y
PDB:
 2GA3
PDB:
 2MLX
PDB:
 2MLY
PDB:
 2MLZ
PDB:
 3BDF
PDB:
 3BDG
PDB:
 3BDH
PDB:
 3CMR
PDB:
 3DPC
PDB:
 3DYC
PDB:
 3TG0
PDB:
 4KM4
PDB:
 4YR1
PDB:
 5C66
PDB:
 5GAD
PDB:
 5GAF
PDB:
 5GAG
PDB:
 5GAH
PDB:
 5JTL
PDB:
 5JTM
PDB:
 5JTN
PDB:
 5JTO
PDB:
 5JTP
PDB:
 5TPQ
PDB:
 6PPT
PDB:
 6PQ2
PDB:
 6PQE
PDB:
 6PQM
PDB:
 6PRI
PDB:
 6PRJ
PDB:
 6PRQ
PDB:
 6PSI
PDB:
 7JM8
PDB:
 7JML
PDB:
 7JMM
PDB:
 7JMZ
PDB:
 7JN8
PDB:
 7JN9
PDB:
 7JNE
PDB:
 7JNG
PFAM:
 PF00245
PRIDE:
 P00634
PRINTS:
 PR00113
PRODB:
 PRO_000023540
PROSITE:
 PS00123
REFSEQ:
 NP_414917
SMART:
 SM00098
SMR:
 P00634
UNIPROT:
 P00634


Operon      
Name: phoA-psiF         
Operon arrangement:
Transcription unit        Promoter
phoA-psiF
psiF


Transcriptional Regulation      
Display Regulation             
Activated by: PhoB


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_495 401433 forward nd [RS-EPT-CBR] [13]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates


Reference(s)    

 [1] Kikuchi Y., Yoda K., Yamasaki M., Tamura G., 1981, The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli., Nucleic Acids Res 9(21):5671-8

 [2] Applebury ML., Johnson BP., Coleman JE., 1970, Phosphate binding to alkaline phosphatase. Metal ion dependence., J Biol Chem 245(19):4968-76

 [3] Ghosh AK., Schramm VL., 2021, Protein Mass-Modulated Effects in Alkaline Phosphatase., Biochemistry 60(2):118-124

 [4] Horiuchi T., Horiuchi S., Mizuno D., 1959, A possible negative feedback phenomenon controlling formation of alkaline phosphomonoesterase in Escherichia coli., Nature 183(4674):1529-30

 [5] Inouye H., Beckwith J., 1977, Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro., Proc Natl Acad Sci U S A 74(4):1440-4

 [6] Le Du MH., Lamoure C., Muller BH., Bulgakov OV., Lajeunesse E., Menez A., Boulain JC., 2002, Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase., J Mol Biol 316(4):941-53

 [7] Ma L., Kantrowitz ER., 1996, Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites., Biochemistry 35(7):2394-402

 [8] Ma L., Tibbitts TT., Kantrowitz ER., 1995, Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites., Protein Sci 4(8):1498-506

 [9] Michaelis S., Inouye H., Oliver D., Beckwith J., 1983, Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli., J Bacteriol 154(1):366-74

 [10] Nesmeyanova MA., Motlokh OB., Kolot MN., Kulaev IS., 1981, Multiple forms of alkaline phosphatase from Escherichia coli cells with repressed and derepressed biosynthesis of the enzyme., J Bacteriol 146(2):453-9

 [11] Schlesinger MJ., 1968, Secretion of alkaline phosphatase subunits by spheroplasts of Escherichia coli., J Bacteriol 96(3):727-33

 [12] Torriani A., 1968, Alkaline phosphatase subunits and their dimerization in vivo., J Bacteriol 96(4):1200-7

 [13] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

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