PPB_ECOLI
ID PPB_ECOLI Reviewed; 471 AA.
AC P00634; P77801; P78051; Q2MC42; Q47041;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Alkaline phosphatase;
DE Short=APase;
DE EC=3.1.3.1;
DE Flags: Precursor;
GN Name=phoA; OrderedLocusNames=b0383, JW0374;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=3537962; DOI=10.1093/nar/14.21.8689;
RA Shuttleworth H., Taylor J., Minton N.;
RT "Sequence of the gene for alkaline phosphatase from Escherichia coli
RT JM83.";
RL Nucleic Acids Res. 14:8689-8689(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3533724; DOI=10.1016/0378-1119(86)90050-8;
RA Chang C.N., Kuang W.-J., Chen E.Y.;
RT "Nucleotide sequence of the alkaline phosphatase gene of Escherichia
RT coli.";
RL Gene 44:121-125(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3045828; DOI=10.1073/pnas.85.18.7036;
RA Dubose R.F., Dykhuizen D.E., Hartl D.L.;
RT "Genetic exchange among natural isolates of bacteria: recombination within
RT the phoA gene of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7036-7040(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
RX PubMed=2345142; DOI=10.1128/jb.172.6.3180-3190.1990;
RA Agrawal D.K., Wanner B.L.;
RT "A phoA structural gene mutation that conditionally affects formation of
RT the enzyme bacterial alkaline phosphatase.";
RL J. Bacteriol. 172:3180-3190(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RX PubMed=6273802; DOI=10.1093/nar/9.21.5671;
RA Kikuchi Y., Yoda K., Yamasaki M., Tamura G.;
RT "The nucleotide sequence of the promoter and the amino-terminal region of
RT alkaline phosphatase structural gene (phoA) of Escherichia coli.";
RL Nucleic Acids Res. 9:5671-5678(1981).
RN [9]
RP PROTEIN SEQUENCE OF 23-471 (ISOZYME 3).
RX PubMed=7022451; DOI=10.1073/pnas.78.6.3473;
RA Bradshaw R.A., Cancedda F., Ericsson L.H., Neumann P.A., Piccoli S.P.,
RA Schlesinger M.J., Shriefer K., Walsh K.A.;
RT "Amino acid sequence of Escherichia coli alkaline phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:3473-3477(1981).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-193 AND 385-399.
RX PubMed=7035431; DOI=10.1128/jb.149.2.434-439.1982;
RA Inouye H., Barnes W., Beckwith J.;
RT "Signal sequence of alkaline phosphatase of Escherichia coli.";
RL J. Bacteriol. 149:434-439(1982).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX PubMed=2668291; DOI=10.1016/s0021-9258(18)71703-1;
RA Laforet G.A., Kaiser E.T., Kendall D.A.;
RT "Signal peptide subsegments are not always functionally interchangeable.
RT M13 procoat hydrophobic core fails to transport alkaline phosphatase in
RT Escherichia coli.";
RL J. Biol. Chem. 264:14478-14485(1989).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=3912261; DOI=10.1016/0378-1119(85)90319-1;
RA Gray G.L., Baldridge J.S., McKeown K.S., Heyneker H.L., Chang C.N.;
RT "Periplasmic production of correctly processed human growth hormone in
RT Escherichia coli: natural and bacterial signal sequences are
RT interchangeable.";
RL Gene 39:247-254(1985).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=3522543; DOI=10.1128/jb.167.1.160-167.1986;
RA Michaelis S., Hunt J.F., Beckwith J.;
RT "Effects of signal sequence mutations on the kinetics of alkaline
RT phosphatase export to the periplasm in Escherichia coli.";
RL J. Bacteriol. 167:160-167(1986).
RN [14]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=3910843; DOI=10.1016/0022-2836(85)90115-9;
RA Sowadski J.M., Handschumacher M.D., Krishna Murthy H.M., Foster B.A.,
RA Wyckoff H.W.;
RT "Refined structure of alkaline phosphatase from Escherichia coli at 2.8-A
RT resolution.";
RL J. Mol. Biol. 186:417-433(1985).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2010919; DOI=10.1016/0022-2836(91)90724-k;
RA Kim E.E., Wyckoff H.W.;
RT "Reaction mechanism of alkaline phosphatase based on crystal structures.
RT Two-metal ion catalysis.";
RL J. Mol. Biol. 218:449-464(1991).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLY-175.
RX PubMed=7577993; DOI=10.1021/bi00043a001;
RA Dealwis C.G., Brennan C., Christianson K., Mandecki W., Abad-Zapatero C.;
RT "Crystallographic analysis of reversible metal binding observed in a mutant
RT (Asp153-->Gly) of Escherichia coli alkaline phosphatase.";
RL Biochemistry 34:13967-13973(1995).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT GLN-434.
RX PubMed=8652582; DOI=10.1021/bi9523421;
RA Ma L., Kantrowitz E.R.;
RT "Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline
RT phosphatase (His-412-->Gln) at one of the zinc binding sites.";
RL Biochemistry 35:2394-2402(1996).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9253408; DOI=10.1038/nsb0897-618;
RA Murphy J.E., Stec B., Ma L., Kantrowitz E.R.;
RT "Trapping and visualization of a covalent enzyme-phosphate intermediate.";
RL Nat. Struct. Biol. 4:618-622(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=9533886; DOI=10.1006/jmbi.1998.1635;
RA Stec B., Hehir M.J., Brennan C., Nolte M., Kantrowitz E.R.;
RT "Kinetic and X-ray structural studies of three mutant E. coli alkaline
RT phosphatases: insights into the catalytic mechanism without the nucleophile
RT Ser102.";
RL J. Mol. Biol. 277:647-662(1998).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10085061; DOI=10.1074/jbc.274.13.8351;
RA Holtz K.M., Stec B., Kantrowitz E.R.;
RT "A model of the transition state in the alkaline phosphatase reaction.";
RL J. Biol. Chem. 274:8351-8354(1999).
RN [22]
RP STRUCTURE BY NMR OF 1-50; 220-310 AND 360-471 IN COMPLEX WITH TRIGGER
RP FACTOR CHAPERONE.
RX PubMed=24812405; DOI=10.1126/science.1250494;
RA Saio T., Guan X., Rossi P., Economou A., Kalodimos C.G.;
RT "Structural basis for protein antiaggregation activity of the trigger
RT factor chaperone.";
RL Science 344:1250494-1250494(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions.;
CC -!- SUBUNIT: Isozymes 1 and 3 are a dimer of identical chains, isozyme 2 is
CC a dimer of heterogeneous chains, one of each of the subunits from
CC isozymes 1 and 3.
CC -!- INTERACTION:
CC P00634; P0AEG4: dsbA; NbExp=2; IntAct=EBI-552958, EBI-549711;
CC P00634; P10408: secA; NbExp=3; IntAct=EBI-552958, EBI-543213;
CC P00634; Q5S007: LRRK2; Xeno; NbExp=2; IntAct=EBI-552958, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR EMBL; X04586; CAA28257.1; -; Genomic_DNA.
DR EMBL; M13345; AAA83893.1; -; Genomic_DNA.
DR EMBL; M29664; AAA24364.1; -; Genomic_DNA.
DR EMBL; M29665; AAA24365.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18107.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73486.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76164.1; -; Genomic_DNA.
DR EMBL; M33536; AAA24372.1; -; Genomic_DNA.
DR EMBL; J01659; AAA24359.2; -; Genomic_DNA.
DR EMBL; J01660; AAA24360.1; -; Genomic_DNA.
DR EMBL; J01661; AAA24361.1; -; Genomic_DNA.
DR EMBL; J05005; AAA24362.1; -; Genomic_DNA.
DR EMBL; M14399; AAA23431.1; -; mRNA.
DR EMBL; M13763; AAA24358.1; -; Genomic_DNA.
DR PIR; A00776; PAECA.
DR RefSeq; NP_414917.2; NC_000913.3.
DR RefSeq; WP_000814403.1; NZ_SSZK01000009.1.
DR PDB; 1AJA; X-ray; 2.50 A; A/B=23-471.
DR PDB; 1AJB; X-ray; 2.50 A; A/B=23-471.
DR PDB; 1AJC; X-ray; 2.50 A; A/B=23-471.
DR PDB; 1AJD; X-ray; 2.50 A; A/B=23-471.
DR PDB; 1ALH; X-ray; 2.50 A; A/B=26-471.
DR PDB; 1ALI; X-ray; 2.20 A; A/B=23-471.
DR PDB; 1ALJ; X-ray; 2.60 A; A/B=23-471.
DR PDB; 1ALK; X-ray; 2.00 A; A/B=23-471.
DR PDB; 1ANI; X-ray; 2.50 A; A/B=26-471.
DR PDB; 1ANJ; X-ray; 2.30 A; A/B=26-471.
DR PDB; 1B8J; X-ray; 1.90 A; A/B=23-471.
DR PDB; 1ED8; X-ray; 1.75 A; A/B=23-471.
DR PDB; 1ED9; X-ray; 1.75 A; A/B=23-471.
DR PDB; 1ELX; X-ray; 2.60 A; A/B=23-471.
DR PDB; 1ELY; X-ray; 2.80 A; A/B=23-471.
DR PDB; 1ELZ; X-ray; 2.80 A; A/B=23-471.
DR PDB; 1EW8; X-ray; 2.20 A; A/B=23-471.
DR PDB; 1EW9; X-ray; 2.00 A; A/B=23-471.
DR PDB; 1HJK; X-ray; 2.30 A; A/B=23-471.
DR PDB; 1HQA; X-ray; 2.25 A; A/B=23-471.
DR PDB; 1KH4; X-ray; 2.40 A; A/B=23-471.
DR PDB; 1KH5; X-ray; 2.00 A; A/B=23-471.
DR PDB; 1KH7; X-ray; 2.40 A; A/B=23-471.
DR PDB; 1KH9; X-ray; 2.50 A; A/B=23-471.
DR PDB; 1KHJ; X-ray; 2.30 A; A/B=23-471.
DR PDB; 1KHK; X-ray; 2.50 A; A/B=23-471.
DR PDB; 1KHL; X-ray; 2.50 A; A/B=23-471.
DR PDB; 1KHN; X-ray; 2.60 A; A/B=23-471.
DR PDB; 1URA; X-ray; 2.04 A; A/B=26-471.
DR PDB; 1URB; X-ray; 2.14 A; A/B=26-471.
DR PDB; 1Y6V; X-ray; 1.60 A; A/B=23-471.
DR PDB; 1Y7A; X-ray; 1.77 A; A/B=23-471.
DR PDB; 2ANH; X-ray; 2.40 A; A/B=26-471.
DR PDB; 2G9Y; X-ray; 2.00 A; A/B=23-471.
DR PDB; 2GA3; X-ray; 2.20 A; A/B=23-471.
DR PDB; 2MLX; NMR; -; B=220-310.
DR PDB; 2MLY; NMR; -; B=1-150.
DR PDB; 2MLZ; NMR; -; B=360-471.
DR PDB; 3BDF; X-ray; 1.40 A; A/B=22-471.
DR PDB; 3BDG; X-ray; 1.40 A; A/B=22-471.
DR PDB; 3BDH; X-ray; 1.85 A; A/B=22-471.
DR PDB; 3CMR; X-ray; 2.05 A; A/B=23-471.
DR PDB; 3DPC; X-ray; 2.30 A; A/B=23-471.
DR PDB; 3DYC; X-ray; 2.30 A; A/B=23-471.
DR PDB; 3TG0; X-ray; 1.20 A; A/B/C/D=23-471.
DR PDB; 4KM4; X-ray; 2.80 A; A/B=26-470.
DR PDB; 4YR1; X-ray; 2.24 A; A/B=31-471.
DR PDB; 5C66; X-ray; 2.03 A; A/B=23-471.
DR PDB; 5GAD; EM; 3.70 A; k=1-18.
DR PDB; 5GAF; EM; 4.30 A; k=1-18.
DR PDB; 5GAG; EM; 3.80 A; k=1-18.
DR PDB; 5GAH; EM; 3.80 A; k=1-18.
DR PDB; 5JTL; NMR; -; E=1-471.
DR PDB; 5JTM; NMR; -; E/F/G/H=1-25.
DR PDB; 5JTN; NMR; -; E/F=91-145.
DR PDB; 5JTO; NMR; -; E/F/G/H=271-310.
DR PDB; 5JTP; NMR; -; E/F/G/H=450-471.
DR PDB; 5TPQ; X-ray; 2.45 A; A/B=30-471.
DR PDB; 6PPT; NMR; -; A=3-13.
DR PDB; 6PQ2; NMR; -; A=10-20.
DR PDB; 6PQE; NMR; -; A=235-245.
DR PDB; 6PQM; NMR; -; A=415-430.
DR PDB; 6PRI; NMR; -; A=437-447.
DR PDB; 6PRJ; NMR; -; A=457-467.
DR PDB; 6PRQ; NMR; -; A=179-187.
DR PDB; 6PSI; NMR; -; B=1-471.
DR PDB; 7JMM; X-ray; 2.56 A; M=63-72.
DR PDB; 7JN8; X-ray; 3.09 A; B=381-390.
DR PDB; 7JN9; X-ray; 2.40 A; B=432-446.
DR PDB; 7JNE; X-ray; 2.54 A; B=435-444.
DR PDB; 7N6J; X-ray; 2.00 A; B=1-19.
DR PDB; 7N6K; X-ray; 2.55 A; B=6-15.
DR PDB; 7N6L; X-ray; 2.40 A; B=270-284.
DR PDB; 7N6M; X-ray; 1.82 A; B=273-282.
DR PDBsum; 1AJA; -.
DR PDBsum; 1AJB; -.
DR PDBsum; 1AJC; -.
DR PDBsum; 1AJD; -.
DR PDBsum; 1ALH; -.
DR PDBsum; 1ALI; -.
DR PDBsum; 1ALJ; -.
DR PDBsum; 1ALK; -.
DR PDBsum; 1ANI; -.
DR PDBsum; 1ANJ; -.
DR PDBsum; 1B8J; -.
DR PDBsum; 1ED8; -.
DR PDBsum; 1ED9; -.
DR PDBsum; 1ELX; -.
DR PDBsum; 1ELY; -.
DR PDBsum; 1ELZ; -.
DR PDBsum; 1EW8; -.
DR PDBsum; 1EW9; -.
DR PDBsum; 1HJK; -.
DR PDBsum; 1HQA; -.
DR PDBsum; 1KH4; -.
DR PDBsum; 1KH5; -.
DR PDBsum; 1KH7; -.
DR PDBsum; 1KH9; -.
DR PDBsum; 1KHJ; -.
DR PDBsum; 1KHK; -.
DR PDBsum; 1KHL; -.
DR PDBsum; 1KHN; -.
DR PDBsum; 1URA; -.
DR PDBsum; 1URB; -.
DR PDBsum; 1Y6V; -.
DR PDBsum; 1Y7A; -.
DR PDBsum; 2ANH; -.
DR PDBsum; 2G9Y; -.
DR PDBsum; 2GA3; -.
DR PDBsum; 2MLX; -.
DR PDBsum; 2MLY; -.
DR PDBsum; 2MLZ; -.
DR PDBsum; 3BDF; -.
DR PDBsum; 3BDG; -.
DR PDBsum; 3BDH; -.
DR PDBsum; 3CMR; -.
DR PDBsum; 3DPC; -.
DR PDBsum; 3DYC; -.
DR PDBsum; 3TG0; -.
DR PDBsum; 4KM4; -.
DR PDBsum; 4YR1; -.
DR PDBsum; 5C66; -.
DR PDBsum; 5GAD; -.
DR PDBsum; 5GAF; -.
DR PDBsum; 5GAG; -.
DR PDBsum; 5GAH; -.
DR PDBsum; 5JTL; -.
DR PDBsum; 5JTM; -.
DR PDBsum; 5JTN; -.
DR PDBsum; 5JTO; -.
DR PDBsum; 5JTP; -.
DR PDBsum; 5TPQ; -.
DR PDBsum; 6PPT; -.
DR PDBsum; 6PQ2; -.
DR PDBsum; 6PQE; -.
DR PDBsum; 6PQM; -.
DR PDBsum; 6PRI; -.
DR PDBsum; 6PRJ; -.
DR PDBsum; 6PRQ; -.
DR PDBsum; 6PSI; -.
DR PDBsum; 7JMM; -.
DR PDBsum; 7JN8; -.
DR PDBsum; 7JN9; -.
DR PDBsum; 7JNE; -.
DR PDBsum; 7N6J; -.
DR PDBsum; 7N6K; -.
DR PDBsum; 7N6L; -.
DR PDBsum; 7N6M; -.
DR AlphaFoldDB; P00634; -.
DR BMRB; P00634; -.
DR PCDDB; P00634; -.
DR SMR; P00634; -.
DR BioGRID; 4259827; 50.
DR DIP; DIP-10496N; -.
DR IntAct; P00634; 7.
DR STRING; 511145.b0383; -.
DR ChEMBL; CHEMBL4217; -.
DR DrugBank; DB04522; Dexfosfoserine.
DR DrugBank; DB03498; Mercaptomethyl Phosphonate.
DR DrugBank; DB02823; Phosphonoacetic Acid.
DR DrugBank; DB04031; Serine vanadate.
DR PaxDb; P00634; -.
DR PRIDE; P00634; -.
DR EnsemblBacteria; AAC73486; AAC73486; b0383.
DR EnsemblBacteria; BAE76164; BAE76164; BAE76164.
DR GeneID; 945041; -.
DR KEGG; ecj:JW0374; -.
DR KEGG; eco:b0383; -.
DR PATRIC; fig|1411691.4.peg.1895; -.
DR EchoBASE; EB0720; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_0_1_6; -.
DR InParanoid; P00634; -.
DR OMA; CANMQVA; -.
DR PhylomeDB; P00634; -.
DR BioCyc; EcoCyc:ALKAPHOSPHA-MON; -.
DR BioCyc; MetaCyc:ALKAPHOSPHA-MON; -.
DR BRENDA; 3.1.3.1; 2026.
DR SABIO-RK; P00634; -.
DR EvolutionaryTrace; P00634; -.
DR PRO; PR:P00634; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:CAFA.
DR GO; GO:0033748; F:hydrogenase (acceptor) activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0030613; F:oxidoreductase activity, acting on phosphorus or arsenic in donors; IDA:EcoliWiki.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0016311; P:dephosphorylation; IDA:EcoCyc.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:CAFA.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Magnesium; Metal-binding; Periplasm; Phosphoprotein; Reference proteome;
KW Signal; Zinc.
FT SIGNAL 1..21
FT CHAIN 22..471
FT /note="Alkaline phosphatase"
FT /id="PRO_0000024012"
FT ACT_SITE 124
FT /note="Phosphoserine intermediate"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT DISULFID 190..200
FT DISULFID 308..358
FT VARIANT 22
FT /note="Missing (in isozyme 3)"
FT CONFLICT 10
FT /note="L -> V (in Ref. 12; AAA23431)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..80
FT /note="SEI -> WGS (in Ref. 8; AAA24359)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="E -> Q (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:7N6J"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:5JTL"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6PSI"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6PSI"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5JTN"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6PSI"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:3TG0"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1ALK"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:3TG0"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:1KH5"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:5JTL"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6PSI"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:1ED9"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1ED8"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6PSI"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 357..381
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3DPC"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:2MLZ"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:3TG0"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:3TG0"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:3TG0"
SQ SEQUENCE 471 AA; 49439 MW; 8A8DE1F29D9D9253 CRC64;
MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD QTAALRDSLS
DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY
VTDSAASATA WSTGVKTYNG ALGVDIHEKD HPTILEMAKA AGLATGNVST AELQDATPAA
LVAHVTSRKC YGPSATSEKC PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG
EWQGKTLREQ AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN
IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK QDHAANPCGQ
IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA PDTKAPGLTQ ALNTKDGAVM
VMSYGNSEED SQEHTGSQLR IAAYGPHAAN VVGLTDQTDL FYTMKAALGL K
