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Entry: PPB_ECOLI
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Original site: 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   24-JAN-2024, entry version 221.
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; Pseudomonadota; 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; 511145-b0383; -.
DR   EnsemblBacteria; AAC73486; AAC73486; b0383.
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; SYHGNID; -.
DR   OrthoDB; 9794455at2; -.
DR   PhylomeDB; P00634; -.
DR   BioCyc; EcoCyc:ALKAPHOSPHA-MONOMER; -.
DR   BioCyc; MetaCyc:ALKAPHOSPHA-MONOMER; -.
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; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 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
//
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