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UniProtKB/Swiss-Prot entry P00634


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PPB_ECOLI
Primary accession number P00634
Secondary accession numbers P77801 P78051 Q2MC42 Q47041
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    October 14, 2008 (Entry version 109)
Name and origin of the protein
Protein name Alkaline phosphatase [Precursor]
Synonyms APase
EC 3.1.3.1
Gene name
Name: phoA
OrderedLocusNames: b0383, JW0374
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35607 / JM83;
DOI=10.1093/nar/14.21.8689; PubMed=3537962 [NCBI, ExPASy, EBI, Israel, Japan]
Shuttleworth H., Taylor J., Minton N.;
"Sequence of the gene for alkaline phosphatase from Escherichia coli JM83.";
Nucleic Acids Res. 14:8689-8689(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(86)90050-8; PubMed=3533724 [NCBI, ExPASy, EBI, Israel, Japan]
Chang C.N., Kuang W.-J., Chen E.Y.;
"Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli.";
Gene 44:121-125(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3045828 [NCBI, ExPASy, EBI, Israel, Japan]
Dubose R.F., Dykhuizen D.E., Hartl D.L.;
"Genetic exchange among natural isolates of bacteria: recombination within the phoA gene of Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 85:7036-7040(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
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.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
PubMed=2345142 [NCBI, ExPASy, EBI, Israel, Japan]
Agrawal D.K., Wanner B.L.;
"A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase.";
J. Bacteriol. 172:3180-3190(1990).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
DOI=10.1093/nar/9.21.5671; PubMed=6273802 [NCBI, ExPASy, EBI, Israel, Japan]
Kikuchi Y., Yoda K., Yamasaki M., Tamura G.;
"The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli.";
Nucleic Acids Res. 9:5671-5678(1981).
[9]
PROTEIN SEQUENCE OF 23-471 (ISOZYME 3).
PubMed=7022451 [NCBI, ExPASy, EBI, Israel, Japan]
Bradshaw R.A., Cancedda F., Ericsson L.H., Neumann P.A., Piccoli S.P., Schlesinger M.J., Shriefer K., Walsh K.A.;
"Amino acid sequence of Escherichia coli alkaline phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 78:3473-3477(1981).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-193 AND 385-399.
PubMed=7035431 [NCBI, ExPASy, EBI, Israel, Japan]
Inouye H., Barnes W., Beckwith J.;
"Signal sequence of alkaline phosphatase of Escherichia coli.";
J. Bacteriol. 149:434-439(1982).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
PubMed=2668291 [NCBI, ExPASy, EBI, Israel, Japan]
Laforet G.A., Kaiser E.T., Kendall D.A.;
"Signal peptide subsegments are not always functionally interchangeable. M13 procoat hydrophobic core fails to transport alkaline phosphatase in Escherichia coli.";
J. Biol. Chem. 264:14478-14485(1989).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
DOI=10.1016/0378-1119(85)90319-1; PubMed=3912261 [NCBI, ExPASy, EBI, Israel, Japan]
Gray G.L., Baldridge J.S., McKeown K.S., Heyneker H.L., Chang C.N.;
"Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable.";
Gene 39:247-254(1985).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
PubMed=3522543 [NCBI, ExPASy, EBI, Israel, Japan]
Michaelis S., Hunt J.F., Beckwith J.;
"Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli.";
J. Bacteriol. 167:160-167(1986).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1016/0022-2836(85)90115-9; PubMed=3910843 [NCBI, ExPASy, EBI, Israel, Japan]
Sowadski J.M., Handschumacher M.D., Krishna Murthy H.M., Foster B.A., Wyckoff H.W.;
"Refined structure of alkaline phosphatase from Escherichia coli at 2.8-A resolution.";
J. Mol. Biol. 186:417-433(1985).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1016/0022-2836(91)90724-K; PubMed=2010919 [NCBI, ExPASy, EBI, Israel, Japan]
Kim E.E., Wyckoff H.W.;
"Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis.";
J. Mol. Biol. 218:449-464(1991).
[16]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLY-175.
DOI=10.1021/bi00043a001; PubMed=7577993 [NCBI, ExPASy, EBI, Israel, Japan]
Dealwis C.G., Brennan C., Christianson K., Mandecki W., Abad-Zapatero C.;
"Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase.";
Biochemistry 34:13967-13973(1995).
[17]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT GLN-434.
DOI=10.1021/bi9523421; PubMed=8652582 [NCBI, ExPASy, EBI, Israel, Japan]
Ma L., Kantrowitz E.R.;
"Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites.";
Biochemistry 35:2394-2402(1996).
[18]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1038/nsb0897-618; PubMed=9253408 [NCBI, ExPASy, EBI, Israel, Japan]
Murphy J.E., Stec B., Ma L., Kantrowitz E.R.;
"Trapping and visualization of a covalent enzyme-phosphate intermediate.";
Nat. Struct. Biol. 4:618-622(1997).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1006/jmbi.1998.1635; PubMed=9533886 [NCBI, ExPASy, EBI, Israel, Japan]
Stec B., Hehir M.J., Brennan C., Nolte M., Kantrowitz E.R.;
"Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102.";
J. Mol. Biol. 277:647-662(1998).
[20]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1074/jbc.274.13.8351; PubMed=10085061 [NCBI, ExPASy, EBI, Israel, Japan]
Holtz K.M., Stec B., Kantrowitz E.R.;
"A model of the transition state in the alkaline phosphatase reaction.";
J. Biol. Chem. 274:8351-8354(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04586; CAA28257.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13345; AAA83893.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29664; AAA24364.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29665; AAA24365.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U73857; AAB18107.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73486.2; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76164.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33536; AAA24372.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J01659; AAA24359.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J01660; AAA24360.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J01661; AAA24361.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J05005; AAA24362.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14399; AAA23431.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13763; AAA24358.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00776; PAECA.
RefSeq AP_001034.1; -.
NP_414917.2; -.
3D structure databases
PDB
1AJA; X-ray; 2.50 A; A/B=23-471.[ExPASy / RCSB / EBI]
1AJB; X-ray; 2.50 A; A/B=23-471.[ExPASy / RCSB / EBI]
1AJC; X-ray; 2.50 A; A/B=23-471.[ExPASy / RCSB / EBI]
1AJD; X-ray; 2.50 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ALH; X-ray; 2.50 A; A/B=26-471.[ExPASy / RCSB / EBI]
1ALI; X-ray; 2.20 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ALJ; X-ray; 2.60 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ALK; X-ray; 2.00 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ANI; X-ray; 2.50 A; A/B=26-471.[ExPASy / RCSB / EBI]
1ANJ; X-ray; 2.30 A; A/B=26-471.[ExPASy / RCSB / EBI]
1B8J; X-ray; 1.90 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ED8; X-ray; 1.75 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ED9; X-ray; 1.75 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ELX; X-ray; 2.60 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ELY; X-ray; 2.80 A; A/B=23-471.[ExPASy / RCSB / EBI]
1ELZ; X-ray; 2.80 A; A/B=23-471.[ExPASy / RCSB / EBI]
1EW8; X-ray; 2.20 A; A/B=23-471.[ExPASy / RCSB / EBI]
1EW9; X-ray; 2.00 A; A/B=23-471.[ExPASy / RCSB / EBI]
1HJK; X-ray; 2.30 A; A/B=23-471.[ExPASy / RCSB / EBI]
1HQA; X-ray; 2.25 A; A/B=23-471.[ExPASy / RCSB / EBI]
1KH4; X-ray; 2.40 A; A/B=23-471.[ExPASy / RCSB / EBI]
1KH5; X-ray; 2.00 A; A/B=23-471.[ExPASy / RCSB / EBI]
1KH7; X-ray; 2.40 A; A/B=23-471.[ExPASy / RCSB / EBI]
1KH9; X-ray; 2.50 A; A/B=23-471.[ExPASy / RCSB / EBI]
1KHJ; X-ray; 2.30 A; A/B=23-471.[ExPASy / RCSB / EBI]
1KHK; X-ray; 2.50 A; A/B=23-471.[ExPASy / RCSB / EBI]
1KHL; X-ray; 2.50 A; A/B=23-471.[ExPASy / RCSB / EBI]
1KHN; X-ray; 2.60 A; A/B=23-471.[ExPASy / RCSB / EBI]
1URA; X-ray; 2.04 A; A/B=26-471.[ExPASy / RCSB / EBI]
1URB; X-ray; 2.14 A; A/B=26-471.[ExPASy / RCSB / EBI]
1Y6V; X-ray; 1.60 A; A/B=23-471.[ExPASy / RCSB / EBI]
1Y7A; X-ray; 1.77 A; A/B=23-471.[ExPASy / RCSB / EBI]
2ANH; X-ray; 2.40 A; A/B=26-471.[ExPASy / RCSB / EBI]
2G9Y; X-ray; 2.00 A; A/B=23-471.[ExPASy / RCSB / EBI]
2GA3; X-ray; 2.20 A; A/B=23-471.[ExPASy / RCSB / EBI]
3CMR; X-ray; 2.05 A; A/B=23-471.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AJA; -.
1AJB; -.
1AJC; -.
1AJD; -.
1ALH; -.
1ALI; -.
1ALJ; -.
1ALK; -.
1ANI; -.
1ANJ; -.
1B8J; -.
1ED8; -.
1ED9; -.
1ELX; -.
1ELY; -.
1ELZ; -.
1EW8; -.
1EW9; -.
1HJK; -.
1HQA; -.
1KH4; -.
1KH5; -.
1KH7; -.
1KH9; -.
1KHJ; -.
1KHK; -.
1KHL; -.
1KHN; -.
1URA; -.
1URB; -.
1Y6V; -.
1Y7A; -.
2ANH; -.
2G9Y; -.
2GA3; -.
3CMR; -.
ModBase P00634.
Protein-protein interaction databases
DIP DIP:10496N; -.
IntAct P00634; -.
Enzyme and pathway databases
BioCyc EcoCyc:ALKAPHOSPHA-MON; -.
MetaCyc:ALKAPHOSPHA-MON; -.
2D gel databases
ECO2DBASE F046.6; 6TH EDITION.
Organism-specific databases
EchoBASE EB0720; -.
EcoGene EG10727; phoA.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR017849; Alkaline_Pase-like_a/b/a.
IPR001952; Alkaline_phosphatase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.720.10; Alk_phosphtse; 1.
Pfam PF00245; Alk_phosphatase; 1.
Pfam graphical view of domain structure.
PRINTS PR00113; ALKPHPHTASE.
SMART SM00098; alkPPc; 1.
SMART graphical view of domain structure.
PROSITE PS00123; ALKALINE_PHOSPHATASE; 1.
BLOCKS P00634.
ProtoNet P00634.
Other
SWISS-3DIMAGE P00634.
Genome annotation databases
GeneID 945041; -.
GenomeReviews U00096_GR; b0383.
AP009048_GR; JW0374.
KEGG ecj:JW0374; -.
eco:b0383; -.
Phylogenomic databases
HOGENOM P00634; -.
Other
LinkHub P00634; -.
Genome annotation databases
CMR P00634; b0383.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Periplasm; Phosphoprotein; Signal; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    21  21      
CHAIN   22   471  450     Alkaline phosphatase. PRO_0000024012
ACT_SITE   124   124        Phosphoserine intermediate. 
METAL   73    73        Magnesium. 
METAL   73    73        Zinc 2. 
METAL   175   175        Magnesium. 
METAL   177   177        Magnesium. 
METAL   344   344        Magnesium. 
METAL   349   349        Zinc 1. 
METAL   353   353        Zinc 1. 
METAL   391   391        Zinc 2. 
METAL   392   392        Zinc 2. 
METAL   434   434        Zinc 1. 
DISULFID   190   200         
DISULFID   308   358         
VARIANT   22    22  1     Missing (in isozyme 3). 
CONFLICT   10    10        L -> V (in Ref. 12; AAA23431). 
CONFLICT   78    80        SEI -> WGS (in Ref. 8; AAA24359). 
CONFLICT   198   198        E -> Q (in Ref. 9; AA sequence). 
TURN   41    44  4      
HELIX   52    56  5      
STRAND   65    72  8      
HELIX   77    88  12      
TURN   95    98  4      
STRAND   101   107  7      
TURN   113   115  3      
STRAND   118   121  4      
HELIX   124   133  10      
STRAND   142   144  3      
HELIX   154   160  7      
STRAND   164   172  9      
HELIX   176   179  4      
TURN   180   182  3      
HELIX   193   199  7      
HELIX   201   203  3      
HELIX   205   207  3      
HELIX   213   220  8      
STRAND   223   228  6      
HELIX   231   234  4      
STRAND   235   240  6      
HELIX   247   253  7      
STRAND   257   259  3      
HELIX   262   267  6      
STRAND   272   275  4      
STRAND   277   280  4      
STRAND   282   285  4      
STRAND   289   291  3      
HELIX   299   302  4      
HELIX   312   314  3      
STRAND   316   318  3      
HELIX   321   333  13      
STRAND   339   345  7      
HELIX   347   353  7      
HELIX   357   381  25      
STRAND   382   393  12      
STRAND   397   399  3      
STRAND   406   413  8      
STRAND   417   424  8      
STRAND   428   431  4      
STRAND   439   445  7      
HELIX   448   451  4      
STRAND   452   456  5      
HELIX   457   467  11      
Sequence information
Length: 471 AA [This is the length of the unprocessed precursor] Molecular weight: 49439 Da [This is the MW of the unprocessed precursor] CRC64: 8A8DE1F29D9D9253 [This is a checksum on the sequence]
        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 

P00634 in FASTA format

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