Reviewed, UniProtKB/Swiss-Prot P00634 (PPB_ECOLI)

Names and origin

Protein names

Recommended name:
    Alkaline phosphatase
      Short name=APase
    EC=3.1.3.1

Gene names

Name:	phoA
Ordered Locus Names:	b0383, JW0374

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate.
Cofactor	Binds 1 magnesium ion. Binds 2 zinc ions.
Subunit structure	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.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the alkaline phosphatase family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Magnesium Metal-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alkaline phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	1	EBI-552958,EBI-542092
secA	P10408	1	EBI-552958,EBI-543213

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 471

450

Alkaline phosphatase

PRO_0000024012

Sites

Active site

124

1

Phosphoserine intermediate

Metal binding

73

1

Magnesium

Metal binding

73

1

Zinc 2

Metal binding

175

1

Magnesium

Metal binding

177

1

Magnesium

Metal binding

344

1

Magnesium

Metal binding

349

1

Zinc 1

Metal binding

353

1

Zinc 1

Metal binding

391

1

Zinc 2

Metal binding

392

1

Zinc 2

Metal binding

434

1

Zinc 1

Amino acid modifications

Disulfide bond

190 ↔ 200

Disulfide bond

308 ↔ 358

Natural variations

Natural variant

22

1

Missing in isozyme 3.

Experimental info

Sequence conflict

10

1

L → V in AAA23431. Ref.12

Sequence conflict

78 – 80

3

SEI → WGS in AAA24359. Ref.8

Sequence conflict

198

1

E → Q AA sequence Ref.9

Secondary structure

1

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471

Helix Strand Turn

Details...

Turn

41 – 44

4

Helix

52 – 56

5

Beta strand

65 – 72

8

Helix

77 – 88

12

Turn

95 – 98

4

Beta strand

101 – 107

7

Turn

113 – 115

3

Beta strand

118 – 121

4

Helix

124 – 133

10

Beta strand

142 – 144

3

Helix

154 – 160

7

Beta strand

164 – 172

9

Helix

176 – 179

4

Turn

180 – 182

3

Helix

193 – 199

7

Helix

201 – 203

3

Helix

205 – 207

3

Helix

213 – 220

8

Beta strand

223 – 228

6

Helix

231 – 234

4

Beta strand

235 – 240

6

Helix

247 – 253

7

Beta strand

257 – 259

3

Helix

262 – 267

6

Beta strand

272 – 275

4

Beta strand

277 – 280

4

Beta strand

282 – 285

4

Beta strand

289 – 291

3

Helix

299 – 302

4

Helix

312 – 314

3

Beta strand

316 – 318

3

Helix

321 – 333

13

Beta strand

339 – 345

7

Helix

347 – 353

7

Helix

357 – 381

25

Beta strand

382 – 393

12

Beta strand

397 – 399

3

Beta strand

406 – 413

8

Beta strand

417 – 424

8

Beta strand

428 – 431

4

Beta strand

439 – 445

7

Helix

448 – 451

4

Beta strand

452 – 456

5

Helix

457 – 467

11

Sequences

	Sequence		Length	Mass (Da)
	P00634-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 8A8DE1F29D9D9253	FASTA	471	49,439
	10 20 30 40 50 60 MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD QTAALRDSLS 70 80 90 100 110 120 DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY 130 140 150 160 170 180 VTDSAASATA WSTGVKTYNG ALGVDIHEKD HPTILEMAKA AGLATGNVST AELQDATPAA 190 200 210 220 230 240 LVAHVTSRKC YGPSATSEKC PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG 250 260 270 280 290 300 EWQGKTLREQ AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN 310 320 330 340 350 360 IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK QDHAANPCGQ 370 380 390 400 410 420 IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA PDTKAPGLTQ ALNTKDGAVM 430 440 450 460 470 VMSYGNSEED SQEHTGSQLR IAAYGPHAAN VVGLTDQTDL FYTMKAALGL K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the gene for alkaline phosphatase from Escherichia coli JM83." Shuttleworth H., Taylor J., Minton N. Nucleic Acids Res. 14:8689-8689(1986) [PubMed: 3537962] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35607 / JM83.
[2]	"Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli." Chang C.N., Kuang W.-J., Chen E.Y. Gene 44:121-125(1986) [PubMed: 3533724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Genetic exchange among natural isolates of bacteria: recombination within the phoA gene of Escherichia coli." Dubose R.F., Dykhuizen D.E., Hartl D.L. Proc. Natl. Acad. Sci. U.S.A. 85:7036-7040(1988) [PubMed: 3045828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Sequence of minutes 4-25 of Escherichia coli." 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. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase." Agrawal D.K., Wanner B.L. J. Bacteriol. 172:3180-3190(1990) [PubMed: 2345142] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
[8]	"The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli." Kikuchi Y., Yoda K., Yamasaki M., Tamura G. Nucleic Acids Res. 9:5671-5678(1981) [PubMed: 6273802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
[9]	"Amino acid sequence of Escherichia coli alkaline phosphatase." Bradshaw R.A., Cancedda F., Ericsson L.H., Neumann P.A., Piccoli S.P., Schlesinger M.J., Shriefer K., Walsh K.A. Proc. Natl. Acad. Sci. U.S.A. 78:3473-3477(1981) [PubMed: 7022451] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-471 (ISOZYME 3).
[10]	"Signal sequence of alkaline phosphatase of Escherichia coli." Inouye H., Barnes W., Beckwith J. J. Bacteriol. 149:434-439(1982) [PubMed: 7035431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-193 AND 385-399.
[11]	"Signal peptide subsegments are not always functionally interchangeable. M13 procoat hydrophobic core fails to transport alkaline phosphatase in Escherichia coli." Laforet G.A., Kaiser E.T., Kendall D.A. J. Biol. Chem. 264:14478-14485(1989) [PubMed: 2668291] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
[12]	"Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable." Gray G.L., Baldridge J.S., McKeown K.S., Heyneker H.L., Chang C.N. Gene 39:247-254(1985) [PubMed: 3912261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[13]	"Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli." Michaelis S., Hunt J.F., Beckwith J. J. Bacteriol. 167:160-167(1986) [PubMed: 3522543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[14]	"Refined structure of alkaline phosphatase from Escherichia coli at 2.8-A resolution." Sowadski J.M., Handschumacher M.D., Krishna Murthy H.M., Foster B.A., Wyckoff H.W. J. Mol. Biol. 186:417-433(1985) [PubMed: 3910843] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[15]	"Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis." Kim E.E., Wyckoff H.W. J. Mol. Biol. 218:449-464(1991) [PubMed: 2010919] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[16]	"Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase." Dealwis C.G., Brennan C., Christianson K., Mandecki W., Abad-Zapatero C. Biochemistry 34:13967-13973(1995) [PubMed: 7577993] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLY-175.
[17]	"Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites." Ma L., Kantrowitz E.R. Biochemistry 35:2394-2402(1996) [PubMed: 8652582] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT GLN-434.
[18]	"Trapping and visualization of a covalent enzyme-phosphate intermediate." Murphy J.E., Stec B., Ma L., Kantrowitz E.R. Nat. Struct. Biol. 4:618-622(1997) [PubMed: 9253408] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[19]	"Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102." Stec B., Hehir M.J., Brennan C., Nolte M., Kantrowitz E.R. J. Mol. Biol. 277:647-662(1998) [PubMed: 9533886] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[20]	"A model of the transition state in the alkaline phosphatase reaction." Holtz K.M., Stec B., Kantrowitz E.R. J. Biol. Chem. 274:8351-8354(1999) [PubMed: 10085061] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X04586 Genomic DNA. Translation: CAA28257.1.
M13345 Genomic DNA. Translation: AAA83893.1.
M29664 Genomic DNA. Translation: AAA24364.1.
M29665 Genomic DNA. Translation: AAA24365.1.
U73857 Genomic DNA. Translation: AAB18107.1.
U00096 Genomic DNA. Translation: AAC73486.2. Different initiation.
AP009048 Genomic DNA. Translation: BAE76164.1.
M33536 Genomic DNA. Translation: AAA24372.1.
J01659 Genomic DNA. Translation: AAA24359.2.
J01660 Genomic DNA. Translation: AAA24360.1.
J01661 Genomic DNA. Translation: AAA24361.1.
J05005 Genomic DNA. Translation: AAA24362.1.
M14399 mRNA. Translation: AAA23431.1.
M13763 Genomic DNA. Translation: AAA24358.1.

PIR

PAECA. A00776.

RefSeq

AP_001034.1.
NP_414917.2.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AJA	X-ray	2.50	A/B	23-471	[»]
1AJB	X-ray	2.50	A/B	23-471	[»]
1AJC	X-ray	2.50	A/B	23-471	[»]
1AJD	X-ray	2.50	A/B	23-471	[»]
1ALH	X-ray	2.50	A/B	26-471	[»]
1ALI	X-ray	2.20	A/B	23-471	[»]
1ALJ	X-ray	2.60	A/B	23-471	[»]
1ALK	X-ray	2.00	A/B	23-471	[»]
1ANI	X-ray	2.50	A/B	26-471	[»]
1ANJ	X-ray	2.30	A/B	26-471	[»]
1B8J	X-ray	1.90	A/B	23-471	[»]
1ED8	X-ray	1.75	A/B	23-471	[»]
1ED9	X-ray	1.75	A/B	23-471	[»]
1ELX	X-ray	2.60	A/B	23-471	[»]
1ELY	X-ray	2.80	A/B	23-471	[»]
1ELZ	X-ray	2.80	A/B	23-471	[»]
1EW8	X-ray	2.20	A/B	23-471	[»]
1EW9	X-ray	2.00	A/B	23-471	[»]
1HJK	X-ray	2.30	A/B	23-471	[»]
1HQA	X-ray	2.25	A/B	23-471	[»]
1KH4	X-ray	2.40	A/B	23-471	[»]
1KH5	X-ray	2.00	A/B	23-471	[»]
1KH7	X-ray	2.40	A/B	23-471	[»]
1KH9	X-ray	2.50	A/B	23-471	[»]
1KHJ	X-ray	2.30	A/B	23-471	[»]
1KHK	X-ray	2.50	A/B	23-471	[»]
1KHL	X-ray	2.50	A/B	23-471	[»]
1KHN	X-ray	2.60	A/B	23-471	[»]
1URA	X-ray	2.04	A/B	26-471	[»]
1URB	X-ray	2.14	A/B	26-471	[»]
1Y6V	X-ray	1.60	A/B	23-471	[»]
1Y7A	X-ray	1.77	A/B	23-471	[»]
2ANH	X-ray	2.40	A/B	26-471	[»]
2G9Y	X-ray	2.00	A/B	23-471	[»]
2GA3	X-ray	2.20	A/B	23-471	[»]
3BDF	X-ray	1.40	A/B	22-471	[»]
3BDG	X-ray	1.40	A	22-471	[»]
			B	22-471	[»]
3BDH	X-ray	1.85	A/B	22-471	[»]
3CMR	X-ray	2.05	A/B	23-471	[»]
3DYC	X-ray	2.30	A/B	23-471	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10496N.

IntAct

P00634. 3 interactions.

2-D gel databases

ECO2DBASE

F046.6. 6TH EDITION.

Genome annotation databases

GeneID

945041.

GenomeReviews

Gene locus JW0374 in contig AP009048_GR.
Gene locus b0383 in contig U00096_GR.

KEGG

ecj:JW0374.
eco:b0383.

Organism-specific databases

EchoBASE

EB0720.

EcoGene

EG10727. phoA.

CMR

Search...

Phylogenomic databases

HOGENOM

P00634.

OMA

P00634. VKQSTIA.

Enzyme and pathway databases

BioCyc

EcoCyc:ALKAPHOSPHA-MON.
MetaCyc:ALKAPHOSPHA-MON.

Family and domain databases

InterPro

IPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
[Graphical view]

Gene3D

G3DSA:3.40.720.10. Alk_phosphtse. 1 hit.

Pfam

PF00245. Alk_phosphatase. 1 hit.
[Graphical view]

PRINTS

PR00113. ALKPHPHTASE.

SMART

SM00098. alkPPc. 1 hit.
[Graphical view]

PROSITE

PS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PPB_ECOLI

Accession

Primary (citable) accession number: P00634
Secondary accession number(s): P77801 , P78051, Q2MC42, Q47041

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)