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 27-MAR-2024, entry version 222. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; AH000890; AAA24359.2; -; Genomic_DNA. DR EMBL; AH000890; AAA24360.1; -; Genomic_DNA. DR EMBL; AH000890; 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 BioGRID; 849430; 1. 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; LRYETHG; -. 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 //