Alkaline phosphatase precursor - Escherichia coli (strain K12)

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P00634 (PPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 151. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference 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 Reference proteome
Gene Ontology (GO)
Cellular_component	periplasmic space Inferred from direct assay PubMed 14269305. Source: EcoCyc
Molecular_function	alkaline phosphatase activity Inferred from direct assay PubMed 13826559. Source: EcoCyc hydrogenase (acceptor) activity Inferred from direct assay PubMed 15148399. Source: EcoCyc magnesium ion binding Inferred from direct assay Ref.15. Source: EcoCyc oxidoreductase activity, acting on phosphorus or arsenic in donors Inferred from direct assay PubMed 15148399. Source: EcoliWiki zinc ion binding Inferred from direct assay PubMed 14487220 Ref.15. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dsbA	P0AEG4	2	EBI-552958,EBI-549711

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Chain

22 – 471

450

Alkaline phosphatase

PRO_0000024012

Sites

Active site

124

Phosphoserine intermediate

Metal binding

Magnesium

Metal binding

Zinc 2

Metal binding

175

Magnesium

Metal binding

177

Magnesium

Metal binding

344

Magnesium

Metal binding

349

Zinc 1

Metal binding

353

Zinc 1

Metal binding

391

Zinc 2

Metal binding

392

Zinc 2

Metal binding

434

Zinc 1

Amino acid modifications

Disulfide bond

190 ↔ 200

Disulfide bond

308 ↔ 358

Natural variations

Natural variant

Missing in isozyme 3.

Experimental info

Sequence conflict

L → V in AAA23431. Ref.12

Sequence conflict

78 – 80

SEI → WGS in AAA24359. Ref.8

Sequence conflict

198

E → Q AA sequence Ref.9

Secondary structure

471

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00634 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 8A8DE1F29D9D9253
Show »

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

« Hide

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[14]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[15]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[16]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[17]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLY-175.
[18]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT GLN-434.
[19]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[20]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[21]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
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

NP_414917.2. NC_000913.2.
YP_488676.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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/B	22-471	[»]
3BDH	X-ray	1.85	A/B	22-471	[»]
3CMR	X-ray	2.05	A/B	23-471	[»]
3DPC	X-ray	2.30	A/B	23-471	[»]
3DYC	X-ray	2.30	A/B	23-471	[»]
3TG0	X-ray	1.20	A/B/C/D	23-471	[»]

ProteinModelPortal

P00634.

SMR

P00634. Positions 28-470.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10496N.

IntAct

P00634. 4 interactions.

MINT

MINT-1283619.

STRING

511145.b0383.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73486; AAC73486; b0383.
BAE76164; BAE76164; BAE76164.

GeneID

12930833.
945041.

KEGG

ecj:Y75_p0372.
eco:b0383.

PATRIC

32115907. VBIEscCol129921_0395.

Organism-specific databases

EchoBASE

EB0720.

EcoGene

EG10727. phoA.

Phylogenomic databases

eggNOG

COG1785.

HOGENOM

HOG000099117.

K01077.

OMA

CPSNALE.

ProtClustDB

PRK10518.

Enzyme and pathway databases

BioCyc

EcoCyc:ALKAPHOSPHA-MONOMER.
ECOL316407:JW0374-MONOMER.
MetaCyc:ALKAPHOSPHA-MONOMER.

SABIO-RK

P00634.

Gene expression databases

Genevestigator

P00634.

Family and domain databases

Gene3D

3.40.720.10. 1 hit.

InterPro

IPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]

Pfam

PF00245. Alk_phosphatase. 2 hits.
[Graphical view]

PRINTS

PR00113. ALKPHPHTASE.

SMART

SM00098. alkPPc. 1 hit.
[Graphical view]

SUPFAM

SSF53649. Alkaline_phosphatase_core. 1 hit.

PROSITE

PS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4217.

EvolutionaryTrace

P00634.

Entry information

Entry name

PPB_ECOLI

Accession

Primary (citable) accession number: P00634
Secondary accession number(s): P77801

Q47041

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 151 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents