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Database: UniProt/SWISS-PROT
Entry: PPB_ECOLI
LinkDB: PPB_ECOLI
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   28-MAR-2018, entry version 191.
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
RT   within 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.,
RA   Mau B., 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
RT   MG1655 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
RT   of 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
RT   of 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;
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;
RA   Laforet G.A., Kaiser E.T., Kendall D.A.;
RT   "Signal peptide subsegments are not always functionally
RT   interchangeable. M13 procoat hydrophobic core fails to transport
RT   alkaline phosphatase in 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.,
RA   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
RT   2.8-A 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
RT   structures. 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.,
RA   Abad-Zapatero C.;
RT   "Crystallographic analysis of reversible metal binding observed in a
RT   mutant (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
RT   alkaline phosphatase (His-412-->Gln) at one of the zinc binding
RT   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
RT   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
RT   nucleophile 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
RT   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: A phosphate monoester + H(2)O = an alcohol +
CC       phosphate. {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
CC       2 is a dimer of heterogeneous chains, one of each of the subunits
CC       from isozymes 1 and 3.
CC   -!- INTERACTION:
CC       P0AEG4:dsbA; NbExp=2; IntAct=EBI-552958, EBI-549711;
CC       Q5S007:LRRK2 (xeno); NbExp=2; IntAct=EBI-552958, EBI-5323863;
CC       P10408:secA; NbExp=3; IntAct=EBI-552958, EBI-543213;
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC       {ECO:0000305}.
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_LN832404.1.
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   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   ProteinModelPortal; P00634; -.
DR   SMR; P00634; -.
DR   BioGrid; 4259827; 50.
DR   DIP; DIP-10496N; -.
DR   IntAct; P00634; 7.
DR   STRING; 316385.ECDH10B_0340; -.
DR   ChEMBL; CHEMBL4217; -.
DR   DrugBank; DB03498; Mercaptomethyl Phosphonate.
DR   DrugBank; DB02823; Phosphonoacetic Acid.
DR   DrugBank; DB04522; Phosphonoserine.
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   EcoGene; EG10727; phoA.
DR   eggNOG; ENOG4105G6Z; Bacteria.
DR   eggNOG; COG1785; LUCA.
DR   HOGENOM; HOG000099117; -.
DR   InParanoid; P00634; -.
DR   KO; K01077; -.
DR   OMA; EHTGTQL; -.
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; -; 1.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; PTHR11596; 2.
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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Hydrolase; Magnesium; Metal-binding; Periplasm;
KW   Phosphoprotein; Reference proteome; Signal; Zinc.
FT   SIGNAL        1     21
FT   CHAIN        22    471       Alkaline phosphatase.
FT                                /FTId=PRO_0000024012.
FT   ACT_SITE    124    124       Phosphoserine intermediate.
FT   METAL        73     73       Magnesium.
FT   METAL        73     73       Zinc 2.
FT   METAL       175    175       Magnesium.
FT   METAL       177    177       Magnesium.
FT   METAL       344    344       Magnesium.
FT   METAL       349    349       Zinc 1.
FT   METAL       353    353       Zinc 1.
FT   METAL       391    391       Zinc 2.
FT   METAL       392    392       Zinc 2.
FT   METAL       434    434       Zinc 1.
FT   DISULFID    190    200
FT   DISULFID    308    358
FT   VARIANT      22     22       Missing (in isozyme 3).
FT   CONFLICT     10     10       L -> V (in Ref. 12; AAA23431).
FT                                {ECO:0000305}.
FT   CONFLICT     78     80       SEI -> WGS (in Ref. 8; AAA24359).
FT                                {ECO:0000305}.
FT   CONFLICT    198    198       E -> Q (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND        3      6       {ECO:0000244|PDB:5JTL}.
FT   TURN         16     18       {ECO:0000244|PDB:5JTL}.
FT   TURN         41     44       {ECO:0000244|PDB:3TG0}.
FT   HELIX        52     58       {ECO:0000244|PDB:3TG0}.
FT   STRAND       65     72       {ECO:0000244|PDB:3TG0}.
FT   HELIX        77     87       {ECO:0000244|PDB:3TG0}.
FT   STRAND       93     96       {ECO:0000244|PDB:5JTN}.
FT   HELIX        97     99       {ECO:0000244|PDB:3TG0}.
FT   STRAND      101    107       {ECO:0000244|PDB:3TG0}.
FT   TURN        113    115       {ECO:0000244|PDB:3TG0}.
FT   STRAND      118    121       {ECO:0000244|PDB:3TG0}.
FT   HELIX       124    133       {ECO:0000244|PDB:3TG0}.
FT   STRAND      142    144       {ECO:0000244|PDB:3TG0}.
FT   HELIX       154    160       {ECO:0000244|PDB:3TG0}.
FT   STRAND      164    172       {ECO:0000244|PDB:3TG0}.
FT   HELIX       176    179       {ECO:0000244|PDB:3TG0}.
FT   TURN        180    182       {ECO:0000244|PDB:3TG0}.
FT   STRAND      185    187       {ECO:0000244|PDB:1ALK}.
FT   HELIX       193    199       {ECO:0000244|PDB:3TG0}.
FT   HELIX       201    203       {ECO:0000244|PDB:3TG0}.
FT   HELIX       205    207       {ECO:0000244|PDB:3TG0}.
FT   HELIX       213    220       {ECO:0000244|PDB:3TG0}.
FT   STRAND      223    228       {ECO:0000244|PDB:3TG0}.
FT   HELIX       231    234       {ECO:0000244|PDB:3TG0}.
FT   STRAND      235    240       {ECO:0000244|PDB:3TG0}.
FT   TURN        241    244       {ECO:0000244|PDB:1KH5}.
FT   HELIX       247    253       {ECO:0000244|PDB:3TG0}.
FT   STRAND      257    259       {ECO:0000244|PDB:3TG0}.
FT   HELIX       262    267       {ECO:0000244|PDB:3TG0}.
FT   STRAND      272    275       {ECO:0000244|PDB:3TG0}.
FT   STRAND      277    280       {ECO:0000244|PDB:3TG0}.
FT   STRAND      282    285       {ECO:0000244|PDB:3TG0}.
FT   STRAND      289    291       {ECO:0000244|PDB:3TG0}.
FT   HELIX       296    298       {ECO:0000244|PDB:5JTL}.
FT   HELIX       299    302       {ECO:0000244|PDB:3TG0}.
FT   HELIX       312    314       {ECO:0000244|PDB:1ED9}.
FT   STRAND      316    318       {ECO:0000244|PDB:1ED8}.
FT   HELIX       321    332       {ECO:0000244|PDB:3TG0}.
FT   STRAND      339    345       {ECO:0000244|PDB:3TG0}.
FT   HELIX       347    353       {ECO:0000244|PDB:3TG0}.
FT   HELIX       357    381       {ECO:0000244|PDB:3TG0}.
FT   STRAND      382    389       {ECO:0000244|PDB:3TG0}.
FT   STRAND      391    393       {ECO:0000244|PDB:3TG0}.
FT   STRAND      397    399       {ECO:0000244|PDB:3TG0}.
FT   STRAND      401    403       {ECO:0000244|PDB:3DPC}.
FT   STRAND      406    413       {ECO:0000244|PDB:3TG0}.
FT   STRAND      417    424       {ECO:0000244|PDB:3TG0}.
FT   STRAND      428    431       {ECO:0000244|PDB:3TG0}.
FT   STRAND      433    435       {ECO:0000244|PDB:2MLZ}.
FT   STRAND      439    445       {ECO:0000244|PDB:3TG0}.
FT   HELIX       448    451       {ECO:0000244|PDB:3TG0}.
FT   STRAND      452    456       {ECO:0000244|PDB:3TG0}.
FT   HELIX       457    467       {ECO:0000244|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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