Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00634 (PPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkaline phosphatase

Short name=APase
EC=3.1.3.1
Gene names
Name:phoA
Ordered Locus Names:b0383, JW0374
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 magnesium ion.

Binds 2 zinc ions.

Subunit structure

Isozymes 1 and 3 are a dimer of identical chains, isozyme 2 is a dimer of heterogeneous chains, one of each of the subunits from isozymes 1 and 3.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the alkaline phosphatase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dsbAP0AEG42EBI-552958,EBI-549711

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 471450Alkaline phosphatase
PRO_0000024012

Sites

Active site1241Phosphoserine intermediate
Metal binding731Magnesium
Metal binding731Zinc 2
Metal binding1751Magnesium
Metal binding1771Magnesium
Metal binding3441Magnesium
Metal binding3491Zinc 1
Metal binding3531Zinc 1
Metal binding3911Zinc 2
Metal binding3921Zinc 2
Metal binding4341Zinc 1

Amino acid modifications

Disulfide bond190 ↔ 200
Disulfide bond308 ↔ 358

Natural variations

Natural variant221Missing in isozyme 3.

Experimental info

Sequence conflict101L → V in AAA23431. Ref.12
Sequence conflict78 – 803SEI → WGS in AAA24359. Ref.8
Sequence conflict1981E → Q AA sequence Ref.9

Secondary structure

........................................................................................... 471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00634 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 8A8DE1F29D9D9253

FASTA47149,439
        10         20         30         40         50         60 
MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD QTAALRDSLS 

        70         80         90        100        110        120 
DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY 

       130        140        150        160        170        180 
VTDSAASATA WSTGVKTYNG ALGVDIHEKD HPTILEMAKA AGLATGNVST AELQDATPAA 

       190        200        210        220        230        240 
LVAHVTSRKC YGPSATSEKC PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG 

       250        260        270        280        290        300 
EWQGKTLREQ AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN 

       310        320        330        340        350        360 
IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK QDHAANPCGQ 

       370        380        390        400        410        420 
IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA PDTKAPGLTQ ALNTKDGAVM 

       430        440        450        460        470 
VMSYGNSEED SQEHTGSQLR IAAYGPHAAN VVGLTDQTDL FYTMKAALGL K 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the gene for alkaline phosphatase from Escherichia coli JM83."
Shuttleworth H., Taylor J., Minton N.
Nucleic Acids Res. 14:8689-8689(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / ATCC 35607 / JM83.
[2]"Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli."
Chang C.N., Kuang W.-J., Chen E.Y.
Gene 44:121-125(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genetic exchange among natural isolates of bacteria: recombination within the phoA gene of Escherichia coli."
Dubose R.F., Dykhuizen D.E., Hartl D.L.
Proc. Natl. Acad. Sci. U.S.A. 85:7036-7040(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase."
Agrawal D.K., Wanner B.L.
J. Bacteriol. 172:3180-3190(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
[8]"The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli."
Kikuchi Y., Yoda K., Yamasaki M., Tamura G.
Nucleic Acids Res. 9:5671-5678(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
[9]"Amino acid sequence of Escherichia coli alkaline phosphatase."
Bradshaw R.A., Cancedda F., Ericsson L.H., Neumann P.A., Piccoli S.P., Schlesinger M.J., Shriefer K., Walsh K.A.
Proc. Natl. Acad. Sci. U.S.A. 78:3473-3477(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-471 (ISOZYME 3).
[10]"Signal sequence of alkaline phosphatase of Escherichia coli."
Inouye H., Barnes W., Beckwith J.
J. Bacteriol. 149:434-439(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-193 AND 385-399.
[11]"Signal peptide subsegments are not always functionally interchangeable. M13 procoat hydrophobic core fails to transport alkaline phosphatase in Escherichia coli."
Laforet G.A., Kaiser E.T., Kendall D.A.
J. Biol. Chem. 264:14478-14485(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
[12]"Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable."
Gray G.L., Baldridge J.S., McKeown K.S., Heyneker H.L., Chang C.N.
Gene 39:247-254(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[13]"Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli."
Michaelis S., Hunt J.F., Beckwith J.
J. Bacteriol. 167:160-167(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[14]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[15]"Refined structure of alkaline phosphatase from Escherichia coli at 2.8-A resolution."
Sowadski J.M., Handschumacher M.D., Krishna Murthy H.M., Foster B.A., Wyckoff H.W.
J. Mol. Biol. 186:417-433(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[16]"Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis."
Kim E.E., Wyckoff H.W.
J. Mol. Biol. 218:449-464(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[17]"Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase."
Dealwis C.G., Brennan C., Christianson K., Mandecki W., Abad-Zapatero C.
Biochemistry 34:13967-13973(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLY-175.
[18]"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., Kantrowitz E.R.
Biochemistry 35:2394-2402(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT GLN-434.
[19]"Trapping and visualization of a covalent enzyme-phosphate intermediate."
Murphy J.E., Stec B., Ma L., Kantrowitz E.R.
Nat. Struct. Biol. 4:618-622(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[20]"Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102."
Stec B., Hehir M.J., Brennan C., Nolte M., Kantrowitz E.R.
J. Mol. Biol. 277:647-662(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[21]"A model of the transition state in the alkaline phosphatase reaction."
Holtz K.M., Stec B., Kantrowitz E.R.
J. Biol. Chem. 274:8351-8354(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04586 Genomic DNA. Translation: CAA28257.1.
M13345 Genomic DNA. Translation: AAA83893.1.
M29664 Genomic DNA. Translation: AAA24364.1.
M29665 Genomic DNA. Translation: AAA24365.1.
U73857 Genomic DNA. Translation: AAB18107.1.
U00096 Genomic DNA. Translation: AAC73486.2.
AP009048 Genomic DNA. Translation: BAE76164.1.
M33536 Genomic DNA. Translation: AAA24372.1.
J01659 Genomic DNA. Translation: AAA24359.2.
J01660 Genomic DNA. Translation: AAA24360.1.
J01661 Genomic DNA. Translation: AAA24361.1.
J05005 Genomic DNA. Translation: AAA24362.1.
M14399 mRNA. Translation: AAA23431.1.
M13763 Genomic DNA. Translation: AAA24358.1.
PIRPAECA. A00776.
RefSeqNP_414917.2. NC_000913.3.
YP_488676.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJAX-ray2.50A/B23-471[»]
1AJBX-ray2.50A/B23-471[»]
1AJCX-ray2.50A/B23-471[»]
1AJDX-ray2.50A/B23-471[»]
1ALHX-ray2.50A/B26-471[»]
1ALIX-ray2.20A/B23-471[»]
1ALJX-ray2.60A/B23-471[»]
1ALKX-ray2.00A/B23-471[»]
1ANIX-ray2.50A/B26-471[»]
1ANJX-ray2.30A/B26-471[»]
1B8JX-ray1.90A/B23-471[»]
1ED8X-ray1.75A/B23-471[»]
1ED9X-ray1.75A/B23-471[»]
1ELXX-ray2.60A/B23-471[»]
1ELYX-ray2.80A/B23-471[»]
1ELZX-ray2.80A/B23-471[»]
1EW8X-ray2.20A/B23-471[»]
1EW9X-ray2.00A/B23-471[»]
1HJKX-ray2.30A/B23-471[»]
1HQAX-ray2.25A/B23-471[»]
1KH4X-ray2.40A/B23-471[»]
1KH5X-ray2.00A/B23-471[»]
1KH7X-ray2.40A/B23-471[»]
1KH9X-ray2.50A/B23-471[»]
1KHJX-ray2.30A/B23-471[»]
1KHKX-ray2.50A/B23-471[»]
1KHLX-ray2.50A/B23-471[»]
1KHNX-ray2.60A/B23-471[»]
1URAX-ray2.04A/B26-471[»]
1URBX-ray2.14A/B26-471[»]
1Y6VX-ray1.60A/B23-471[»]
1Y7AX-ray1.77A/B23-471[»]
2ANHX-ray2.40A/B26-471[»]
2G9YX-ray2.00A/B23-471[»]
2GA3X-ray2.20A/B23-471[»]
2MLZNMR-B360-471[»]
3BDFX-ray1.40A/B22-471[»]
3BDGX-ray1.40A/B22-471[»]
3BDHX-ray1.85A/B22-471[»]
3CMRX-ray2.05A/B23-471[»]
3DPCX-ray2.30A/B23-471[»]
3DYCX-ray2.30A/B23-471[»]
3TG0X-ray1.20A/B/C/D23-471[»]
4KM4X-ray2.80A/B26-470[»]
ProteinModelPortalP00634.
SMRP00634. Positions 28-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10496N.
IntActP00634. 4 interactions.
MINTMINT-1283619.
STRING511145.b0383.

Chemistry

ChEMBLCHEMBL4217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73486; AAC73486; b0383.
BAE76164; BAE76164; BAE76164.
GeneID12930833.
945041.
KEGGecj:Y75_p0372.
eco:b0383.
PATRIC32115907. VBIEscCol129921_0395.

Organism-specific databases

EchoBASEEB0720.
EcoGeneEG10727. phoA.

Phylogenomic databases

eggNOGCOG1785.
HOGENOMHOG000099117.
KOK01077.
OMADKGFFLQ.
OrthoDBEOG661H4G.
PhylomeDBP00634.

Enzyme and pathway databases

BioCycEcoCyc:ALKAPHOSPHA-MONOMER.
ECOL316407:JW0374-MONOMER.
MetaCyc:ALKAPHOSPHA-MONOMER.
SABIO-RKP00634.

Gene expression databases

GenevestigatorP00634.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamPF00245. Alk_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00113. ALKPHPHTASE.
SMARTSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00634.
PROP00634.

Entry information

Entry namePPB_ECOLI
AccessionPrimary (citable) accession number: P00634
Secondary accession number(s): P77801 expand/collapse secondary AC list , P78051, Q2MC42, Q47041
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 160 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene