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Alkaline phosphatase (APase) (EC 3.1.3.1)

 PPB_ECOLI               Reviewed;         471 AA.
P00634; P77801; P78051; Q2MC42; Q47041;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
30-AUG-2017, entry version 186.
RecName: Full=Alkaline phosphatase;
Short=APase;
EC=3.1.3.1;
Flags: Precursor;
Name=phoA; OrderedLocusNames=b0383, JW0374;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / ATCC 35607 / JM83;
PubMed=3537962; DOI=10.1093/nar/14.21.8689;
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].
PubMed=3533724; DOI=10.1016/0378-1119(86)90050-8;
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; DOI=10.1073/pnas.85.18.7036;
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;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
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; DOI=10.1128/jb.172.6.3180-3190.1990;
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.
PubMed=6273802; DOI=10.1093/nar/9.21.5671;
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; DOI=10.1073/pnas.78.6.3473;
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;
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;
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.
PubMed=3912261; DOI=10.1016/0378-1119(85)90319-1;
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; DOI=10.1128/jb.167.1.160-167.1986;
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]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=3910843; DOI=10.1016/0022-2836(85)90115-9;
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).
[16]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=2010919; DOI=10.1016/0022-2836(91)90724-K;
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).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLY-175.
PubMed=7577993; DOI=10.1021/bi00043a001;
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).
[18]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT GLN-434.
PubMed=8652582; DOI=10.1021/bi9523421;
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).
[19]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=9253408; DOI=10.1038/nsb0897-618;
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).
[20]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=9533886; DOI=10.1006/jmbi.1998.1635;
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).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=10085061; DOI=10.1074/jbc.274.13.8351;
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).
[22]
STRUCTURE BY NMR OF 1-50; 220-310 AND 360-471 IN COMPLEX WITH TRIGGER
FACTOR CHAPERONE.
PubMed=24812405; DOI=10.1126/science.1250494;
Saio T., Guan X., Rossi P., Economou A., Kalodimos C.G.;
"Structural basis for protein antiaggregation activity of the trigger
factor chaperone.";
Science 344:1250494-1250494(2014).
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) ion.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions.;
-!- SUBUNIT: Isozymes 1 and 3 are a dimer of identical chains, isozyme
2 is a dimer of heterogeneous chains, one of each of the subunits
from isozymes 1 and 3.
-!- INTERACTION:
P0AEG4:dsbA; NbExp=2; IntAct=EBI-552958, EBI-549711;
Q5S007:LRRK2 (xeno); NbExp=2; IntAct=EBI-552958, EBI-5323863;
-!- SUBCELLULAR LOCATION: Periplasm.
-!- SIMILARITY: Belongs to the alkaline phosphatase family.
{ECO:0000305}.
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EMBL; X04586; CAA28257.1; -; Genomic_DNA.
EMBL; M13345; AAA83893.1; -; Genomic_DNA.
EMBL; M29664; AAA24364.1; -; Genomic_DNA.
EMBL; M29665; AAA24365.1; -; Genomic_DNA.
EMBL; U73857; AAB18107.1; -; Genomic_DNA.
EMBL; U00096; AAC73486.2; -; Genomic_DNA.
EMBL; AP009048; BAE76164.1; -; Genomic_DNA.
EMBL; M33536; AAA24372.1; -; Genomic_DNA.
EMBL; J01659; AAA24359.2; -; Genomic_DNA.
EMBL; J01660; AAA24360.1; -; Genomic_DNA.
EMBL; J01661; AAA24361.1; -; Genomic_DNA.
EMBL; J05005; AAA24362.1; -; Genomic_DNA.
EMBL; M14399; AAA23431.1; -; mRNA.
EMBL; M13763; AAA24358.1; -; Genomic_DNA.
PIR; A00776; PAECA.
RefSeq; NP_414917.2; NC_000913.3.
RefSeq; WP_000814403.1; NZ_LN832404.1.
PDB; 1AJA; X-ray; 2.50 A; A/B=23-471.
PDB; 1AJB; X-ray; 2.50 A; A/B=23-471.
PDB; 1AJC; X-ray; 2.50 A; A/B=23-471.
PDB; 1AJD; X-ray; 2.50 A; A/B=23-471.
PDB; 1ALH; X-ray; 2.50 A; A/B=26-471.
PDB; 1ALI; X-ray; 2.20 A; A/B=23-471.
PDB; 1ALJ; X-ray; 2.60 A; A/B=23-471.
PDB; 1ALK; X-ray; 2.00 A; A/B=23-471.
PDB; 1ANI; X-ray; 2.50 A; A/B=26-471.
PDB; 1ANJ; X-ray; 2.30 A; A/B=26-471.
PDB; 1B8J; X-ray; 1.90 A; A/B=23-471.
PDB; 1ED8; X-ray; 1.75 A; A/B=23-471.
PDB; 1ED9; X-ray; 1.75 A; A/B=23-471.
PDB; 1ELX; X-ray; 2.60 A; A/B=23-471.
PDB; 1ELY; X-ray; 2.80 A; A/B=23-471.
PDB; 1ELZ; X-ray; 2.80 A; A/B=23-471.
PDB; 1EW8; X-ray; 2.20 A; A/B=23-471.
PDB; 1EW9; X-ray; 2.00 A; A/B=23-471.
PDB; 1HJK; X-ray; 2.30 A; A/B=23-471.
PDB; 1HQA; X-ray; 2.25 A; A/B=23-471.
PDB; 1KH4; X-ray; 2.40 A; A/B=23-471.
PDB; 1KH5; X-ray; 2.00 A; A/B=23-471.
PDB; 1KH7; X-ray; 2.40 A; A/B=23-471.
PDB; 1KH9; X-ray; 2.50 A; A/B=23-471.
PDB; 1KHJ; X-ray; 2.30 A; A/B=23-471.
PDB; 1KHK; X-ray; 2.50 A; A/B=23-471.
PDB; 1KHL; X-ray; 2.50 A; A/B=23-471.
PDB; 1KHN; X-ray; 2.60 A; A/B=23-471.
PDB; 1URA; X-ray; 2.04 A; A/B=26-471.
PDB; 1URB; X-ray; 2.14 A; A/B=26-471.
PDB; 1Y6V; X-ray; 1.60 A; A/B=23-471.
PDB; 1Y7A; X-ray; 1.77 A; A/B=23-471.
PDB; 2ANH; X-ray; 2.40 A; A/B=26-471.
PDB; 2G9Y; X-ray; 2.00 A; A/B=23-471.
PDB; 2GA3; X-ray; 2.20 A; A/B=23-471.
PDB; 2MLX; NMR; -; B=220-310.
PDB; 2MLY; NMR; -; B=1-150.
PDB; 2MLZ; NMR; -; B=360-471.
PDB; 3BDF; X-ray; 1.40 A; A/B=22-471.
PDB; 3BDG; X-ray; 1.40 A; A/B=22-471.
PDB; 3BDH; X-ray; 1.85 A; A/B=22-471.
PDB; 3CMR; X-ray; 2.05 A; A/B=23-471.
PDB; 3DPC; X-ray; 2.30 A; A/B=23-471.
PDB; 3DYC; X-ray; 2.30 A; A/B=23-471.
PDB; 3TG0; X-ray; 1.20 A; A/B/C/D=23-471.
PDB; 4KM4; X-ray; 2.80 A; A/B=26-470.
PDB; 4YR1; X-ray; 2.24 A; A/B=31-471.
PDB; 5C66; X-ray; 2.03 A; A/B=23-471.
PDB; 5GAD; EM; 3.70 A; k=1-18.
PDB; 5GAF; EM; 4.30 A; k=1-18.
PDB; 5GAG; EM; 3.80 A; k=1-18.
PDB; 5GAH; EM; 3.80 A; k=1-18.
PDB; 5JTL; NMR; -; E=1-471.
PDB; 5JTM; NMR; -; E/F/G/H=1-25.
PDB; 5JTN; NMR; -; E/F=91-145.
PDB; 5JTO; NMR; -; E/F/G/H=271-310.
PDB; 5JTP; NMR; -; E/F/G/H=450-471.
PDBsum; 1AJA; -.
PDBsum; 1AJB; -.
PDBsum; 1AJC; -.
PDBsum; 1AJD; -.
PDBsum; 1ALH; -.
PDBsum; 1ALI; -.
PDBsum; 1ALJ; -.
PDBsum; 1ALK; -.
PDBsum; 1ANI; -.
PDBsum; 1ANJ; -.
PDBsum; 1B8J; -.
PDBsum; 1ED8; -.
PDBsum; 1ED9; -.
PDBsum; 1ELX; -.
PDBsum; 1ELY; -.
PDBsum; 1ELZ; -.
PDBsum; 1EW8; -.
PDBsum; 1EW9; -.
PDBsum; 1HJK; -.
PDBsum; 1HQA; -.
PDBsum; 1KH4; -.
PDBsum; 1KH5; -.
PDBsum; 1KH7; -.
PDBsum; 1KH9; -.
PDBsum; 1KHJ; -.
PDBsum; 1KHK; -.
PDBsum; 1KHL; -.
PDBsum; 1KHN; -.
PDBsum; 1URA; -.
PDBsum; 1URB; -.
PDBsum; 1Y6V; -.
PDBsum; 1Y7A; -.
PDBsum; 2ANH; -.
PDBsum; 2G9Y; -.
PDBsum; 2GA3; -.
PDBsum; 2MLX; -.
PDBsum; 2MLY; -.
PDBsum; 2MLZ; -.
PDBsum; 3BDF; -.
PDBsum; 3BDG; -.
PDBsum; 3BDH; -.
PDBsum; 3CMR; -.
PDBsum; 3DPC; -.
PDBsum; 3DYC; -.
PDBsum; 3TG0; -.
PDBsum; 4KM4; -.
PDBsum; 4YR1; -.
PDBsum; 5C66; -.
PDBsum; 5GAD; -.
PDBsum; 5GAF; -.
PDBsum; 5GAG; -.
PDBsum; 5GAH; -.
PDBsum; 5JTL; -.
PDBsum; 5JTM; -.
PDBsum; 5JTN; -.
PDBsum; 5JTO; -.
PDBsum; 5JTP; -.
ProteinModelPortal; P00634; -.
SMR; P00634; -.
BioGrid; 4259827; 31.
DIP; DIP-10496N; -.
IntAct; P00634; 5.
MINT; MINT-1283619; -.
STRING; 316385.ECDH10B_0340; -.
ChEMBL; CHEMBL4217; -.
DrugBank; DB03498; Mercaptomethyl Phosphonate.
DrugBank; DB02823; Phosphonoacetic Acid.
DrugBank; DB04522; Phosphonoserine.
DrugBank; DB04031; Serine Vanadate.
PaxDb; P00634; -.
PRIDE; P00634; -.
EnsemblBacteria; AAC73486; AAC73486; b0383.
EnsemblBacteria; BAE76164; BAE76164; BAE76164.
GeneID; 945041; -.
KEGG; ecj:JW0374; -.
KEGG; eco:b0383; -.
PATRIC; fig|1411691.4.peg.1895; -.
EchoBASE; EB0720; -.
EcoGene; EG10727; phoA.
eggNOG; ENOG4105G6Z; Bacteria.
eggNOG; COG1785; LUCA.
HOGENOM; HOG000099117; -.
InParanoid; P00634; -.
KO; K01077; -.
PhylomeDB; P00634; -.
BioCyc; EcoCyc:ALKAPHOSPHA-MONOMER; -.
BioCyc; MetaCyc:ALKAPHOSPHA-MONOMER; -.
BRENDA; 3.1.3.1; 2026.
SABIO-RK; P00634; -.
EvolutionaryTrace; P00634; -.
PRO; PR:P00634; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:CAFA.
GO; GO:0033748; F:hydrogenase (acceptor) activity; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0030613; F:oxidoreductase activity, acting on phosphorus or arsenic in donors; IDA:EcoliWiki.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:CAFA.
GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
GO; GO:0016311; P:dephosphorylation; IDA:EcoCyc.
GO; GO:0006470; P:protein dephosphorylation; IDA:CAFA.
CDD; cd16012; ALP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR001952; Alkaline_phosphatase.
InterPro; IPR018299; Alkaline_phosphatase_AS.
InterPro; IPR017850; Alkaline_phosphatase_core.
PANTHER; PTHR11596; PTHR11596; 1.
Pfam; PF00245; Alk_phosphatase; 1.
PRINTS; PR00113; ALKPHPHTASE.
SMART; SM00098; alkPPc; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Hydrolase; Magnesium; Metal-binding; Periplasm;
Phosphoprotein; Reference proteome; Signal; Zinc.
SIGNAL 1 21
CHAIN 22 471 Alkaline phosphatase.
/FTId=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 Missing (in isozyme 3).
CONFLICT 10 10 L -> V (in Ref. 12; AAA23431).
{ECO:0000305}.
CONFLICT 78 80 SEI -> WGS (in Ref. 8; AAA24359).
{ECO:0000305}.
CONFLICT 198 198 E -> Q (in Ref. 9; AA sequence).
{ECO:0000305}.
STRAND 3 6 {ECO:0000244|PDB:5JTL}.
TURN 16 18 {ECO:0000244|PDB:5JTL}.
TURN 41 44 {ECO:0000244|PDB:3TG0}.
HELIX 52 58 {ECO:0000244|PDB:3TG0}.
STRAND 65 72 {ECO:0000244|PDB:3TG0}.
HELIX 77 87 {ECO:0000244|PDB:3TG0}.
STRAND 93 96 {ECO:0000244|PDB:5JTN}.
HELIX 97 99 {ECO:0000244|PDB:3TG0}.
STRAND 101 107 {ECO:0000244|PDB:3TG0}.
TURN 113 115 {ECO:0000244|PDB:3TG0}.
STRAND 118 121 {ECO:0000244|PDB:3TG0}.
HELIX 124 133 {ECO:0000244|PDB:3TG0}.
STRAND 142 144 {ECO:0000244|PDB:3TG0}.
HELIX 154 160 {ECO:0000244|PDB:3TG0}.
STRAND 164 172 {ECO:0000244|PDB:3TG0}.
HELIX 176 179 {ECO:0000244|PDB:3TG0}.
TURN 180 182 {ECO:0000244|PDB:3TG0}.
STRAND 185 187 {ECO:0000244|PDB:1ALK}.
HELIX 193 199 {ECO:0000244|PDB:3TG0}.
HELIX 201 203 {ECO:0000244|PDB:3TG0}.
HELIX 205 207 {ECO:0000244|PDB:3TG0}.
HELIX 213 220 {ECO:0000244|PDB:3TG0}.
STRAND 223 228 {ECO:0000244|PDB:3TG0}.
HELIX 231 234 {ECO:0000244|PDB:3TG0}.
STRAND 235 240 {ECO:0000244|PDB:3TG0}.
TURN 241 244 {ECO:0000244|PDB:1KH5}.
HELIX 247 253 {ECO:0000244|PDB:3TG0}.
STRAND 257 259 {ECO:0000244|PDB:3TG0}.
HELIX 262 267 {ECO:0000244|PDB:3TG0}.
STRAND 272 275 {ECO:0000244|PDB:3TG0}.
STRAND 277 280 {ECO:0000244|PDB:3TG0}.
STRAND 282 285 {ECO:0000244|PDB:3TG0}.
STRAND 289 291 {ECO:0000244|PDB:3TG0}.
HELIX 296 298 {ECO:0000244|PDB:5JTL}.
HELIX 299 302 {ECO:0000244|PDB:3TG0}.
HELIX 312 314 {ECO:0000244|PDB:1ED9}.
STRAND 316 318 {ECO:0000244|PDB:1ED8}.
HELIX 321 332 {ECO:0000244|PDB:3TG0}.
STRAND 339 345 {ECO:0000244|PDB:3TG0}.
HELIX 347 353 {ECO:0000244|PDB:3TG0}.
HELIX 357 381 {ECO:0000244|PDB:3TG0}.
STRAND 382 389 {ECO:0000244|PDB:3TG0}.
STRAND 391 393 {ECO:0000244|PDB:3TG0}.
STRAND 397 399 {ECO:0000244|PDB:3TG0}.
STRAND 401 403 {ECO:0000244|PDB:3DPC}.
STRAND 406 413 {ECO:0000244|PDB:3TG0}.
STRAND 417 424 {ECO:0000244|PDB:3TG0}.
STRAND 428 431 {ECO:0000244|PDB:3TG0}.
STRAND 433 435 {ECO:0000244|PDB:2MLZ}.
STRAND 439 445 {ECO:0000244|PDB:3TG0}.
HELIX 448 451 {ECO:0000244|PDB:3TG0}.
STRAND 452 456 {ECO:0000244|PDB:3TG0}.
HELIX 457 467 {ECO:0000244|PDB:3TG0}.
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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