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P00634

- PPB_ECOLI

UniProt

P00634 - PPB_ECOLI

Protein

Alkaline phosphatase

Gene

phoA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.PROSITE-ProRule annotation

    Cofactori

    Binds 1 magnesium ion.
    Binds 2 zinc ions.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi73 – 731Magnesium
    Metal bindingi73 – 731Zinc 2
    Active sitei124 – 1241Phosphoserine intermediate
    Metal bindingi175 – 1751Magnesium
    Metal bindingi177 – 1771Magnesium
    Metal bindingi344 – 3441Magnesium
    Metal bindingi349 – 3491Zinc 1
    Metal bindingi353 – 3531Zinc 1
    Metal bindingi391 – 3911Zinc 2
    Metal bindingi392 – 3921Zinc 2
    Metal bindingi434 – 4341Zinc 1

    GO - Molecular functioni

    1. alkaline phosphatase activity Source: EcoCyc
    2. hydrogenase (acceptor) activity Source: EcoCyc
    3. magnesium ion binding Source: EcoCyc
    4. oxidoreductase activity, acting on phosphorus or arsenic in donors Source: EcoliWiki
    5. protein binding Source: IntAct
    6. zinc ion binding Source: EcoCyc

    GO - Biological processi

    1. dephosphorylation Source: EcoCyc
    2. oxidation-reduction process Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:ALKAPHOSPHA-MONOMER.
    ECOL316407:JW0374-MONOMER.
    MetaCyc:ALKAPHOSPHA-MONOMER.
    SABIO-RKP00634.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alkaline phosphatase (EC:3.1.3.1)
    Short name:
    APase
    Gene namesi
    Name:phoA
    Ordered Locus Names:b0383, JW0374
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10727. phoA.

    Subcellular locationi

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: EcoCyc
    2. periplasmic space Source: EcoCyc

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 471450Alkaline phosphatasePRO_0000024012Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi190 ↔ 200
    Disulfide bondi308 ↔ 358

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Expressioni

    Gene expression databases

    GenevestigatoriP00634.

    Interactioni

    Subunit structurei

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dsbAP0AEG42EBI-552958,EBI-549711

    Protein-protein interaction databases

    DIPiDIP-10496N.
    IntActiP00634. 4 interactions.
    MINTiMINT-1283619.
    STRINGi511145.b0383.

    Structurei

    Secondary structure

    1
    471
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni41 – 444
    Helixi52 – 587
    Beta strandi65 – 728
    Helixi77 – 8711
    Helixi97 – 993
    Beta strandi101 – 1077
    Turni113 – 1153
    Beta strandi118 – 1214
    Helixi124 – 13310
    Beta strandi142 – 1443
    Helixi154 – 1607
    Beta strandi164 – 1729
    Helixi176 – 1794
    Turni180 – 1823
    Beta strandi185 – 1873
    Helixi193 – 1997
    Helixi201 – 2033
    Helixi205 – 2073
    Helixi213 – 2208
    Beta strandi223 – 2286
    Helixi231 – 2344
    Beta strandi235 – 2406
    Turni241 – 2444
    Helixi247 – 2537
    Beta strandi257 – 2593
    Helixi262 – 2676
    Beta strandi272 – 2754
    Beta strandi277 – 2804
    Beta strandi282 – 2854
    Beta strandi289 – 2913
    Helixi299 – 3024
    Helixi312 – 3143
    Beta strandi316 – 3183
    Helixi321 – 33212
    Beta strandi339 – 3457
    Helixi347 – 3537
    Helixi357 – 38125
    Beta strandi382 – 3898
    Beta strandi391 – 3933
    Beta strandi397 – 3993
    Beta strandi401 – 4033
    Beta strandi406 – 4138
    Beta strandi417 – 4248
    Beta strandi428 – 4314
    Beta strandi433 – 4353
    Beta strandi439 – 4457
    Helixi448 – 4514
    Beta strandi452 – 4565
    Helixi457 – 46711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AJAX-ray2.50A/B23-471[»]
    1AJBX-ray2.50A/B23-471[»]
    1AJCX-ray2.50A/B23-471[»]
    1AJDX-ray2.50A/B23-471[»]
    1ALHX-ray2.50A/B26-471[»]
    1ALIX-ray2.20A/B23-471[»]
    1ALJX-ray2.60A/B23-471[»]
    1ALKX-ray2.00A/B23-471[»]
    1ANIX-ray2.50A/B26-471[»]
    1ANJX-ray2.30A/B26-471[»]
    1B8JX-ray1.90A/B23-471[»]
    1ED8X-ray1.75A/B23-471[»]
    1ED9X-ray1.75A/B23-471[»]
    1ELXX-ray2.60A/B23-471[»]
    1ELYX-ray2.80A/B23-471[»]
    1ELZX-ray2.80A/B23-471[»]
    1EW8X-ray2.20A/B23-471[»]
    1EW9X-ray2.00A/B23-471[»]
    1HJKX-ray2.30A/B23-471[»]
    1HQAX-ray2.25A/B23-471[»]
    1KH4X-ray2.40A/B23-471[»]
    1KH5X-ray2.00A/B23-471[»]
    1KH7X-ray2.40A/B23-471[»]
    1KH9X-ray2.50A/B23-471[»]
    1KHJX-ray2.30A/B23-471[»]
    1KHKX-ray2.50A/B23-471[»]
    1KHLX-ray2.50A/B23-471[»]
    1KHNX-ray2.60A/B23-471[»]
    1URAX-ray2.04A/B26-471[»]
    1URBX-ray2.14A/B26-471[»]
    1Y6VX-ray1.60A/B23-471[»]
    1Y7AX-ray1.77A/B23-471[»]
    2ANHX-ray2.40A/B26-471[»]
    2G9YX-ray2.00A/B23-471[»]
    2GA3X-ray2.20A/B23-471[»]
    2MLZNMR-B360-471[»]
    3BDFX-ray1.40A/B22-471[»]
    3BDGX-ray1.40A/B22-471[»]
    3BDHX-ray1.85A/B22-471[»]
    3CMRX-ray2.05A/B23-471[»]
    3DPCX-ray2.30A/B23-471[»]
    3DYCX-ray2.30A/B23-471[»]
    3TG0X-ray1.20A/B/C/D23-471[»]
    4KM4X-ray2.80A/B26-470[»]
    ProteinModelPortaliP00634.
    SMRiP00634. Positions 28-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00634.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alkaline phosphatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1785.
    HOGENOMiHOG000099117.
    KOiK01077.
    OMAiDKGFFLQ.
    OrthoDBiEOG661H4G.
    PhylomeDBiP00634.

    Family and domain databases

    Gene3Di3.40.720.10. 1 hit.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR001952. Alkaline_phosphatase.
    IPR018299. Alkaline_phosphatase_AS.
    IPR017850. Alkaline_phosphatase_core.
    [Graphical view]
    PfamiPF00245. Alk_phosphatase. 2 hits.
    [Graphical view]
    PRINTSiPR00113. ALKPHPHTASE.
    SMARTiSM00098. alkPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF53649. SSF53649. 1 hit.
    PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00634-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD    50
    QTAALRDSLS DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL 100
    PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVDIHEKD 150
    HPTILEMAKA AGLATGNVST AELQDATPAA LVAHVTSRKC YGPSATSEKC 200
    PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG EWQGKTLREQ 250
    AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN 300
    IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK 350
    QDHAANPCGQ IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA 400
    PDTKAPGLTQ ALNTKDGAVM VMSYGNSEED SQEHTGSQLR IAAYGPHAAN 450
    VVGLTDQTDL FYTMKAALGL K 471
    Length:471
    Mass (Da):49,439
    Last modified:August 13, 1987 - v1
    Checksum:i8A8DE1F29D9D9253
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101L → V in AAA23431. (PubMed:3912261)Curated
    Sequence conflicti78 – 803SEI → WGS in AAA24359. (PubMed:6273802)Curated
    Sequence conflicti198 – 1981E → Q AA sequence (PubMed:7022451)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221Missing in isozyme 3.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA00776. PAECA.
    RefSeqiNP_414917.2. NC_000913.3.
    YP_488676.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73486; AAC73486; b0383.
    BAE76164; BAE76164; BAE76164.
    GeneIDi12930833.
    945041.
    KEGGiecj:Y75_p0372.
    eco:b0383.
    PATRICi32115907. VBIEscCol129921_0395.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A00776. PAECA.
    RefSeqi NP_414917.2. NC_000913.3.
    YP_488676.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    2MLZ NMR - B 360-471 [» ]
    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 [» ]
    4KM4 X-ray 2.80 A/B 26-470 [» ]
    ProteinModelPortali P00634.
    SMRi P00634. Positions 28-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10496N.
    IntActi P00634. 4 interactions.
    MINTi MINT-1283619.
    STRINGi 511145.b0383.

    Chemistry

    ChEMBLi CHEMBL4217.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73486 ; AAC73486 ; b0383 .
    BAE76164 ; BAE76164 ; BAE76164 .
    GeneIDi 12930833.
    945041.
    KEGGi ecj:Y75_p0372.
    eco:b0383.
    PATRICi 32115907. VBIEscCol129921_0395.

    Organism-specific databases

    EchoBASEi EB0720.
    EcoGenei EG10727. phoA.

    Phylogenomic databases

    eggNOGi COG1785.
    HOGENOMi HOG000099117.
    KOi K01077.
    OMAi DKGFFLQ.
    OrthoDBi EOG661H4G.
    PhylomeDBi P00634.

    Enzyme and pathway databases

    BioCyci EcoCyc:ALKAPHOSPHA-MONOMER.
    ECOL316407:JW0374-MONOMER.
    MetaCyc:ALKAPHOSPHA-MONOMER.
    SABIO-RK P00634.

    Miscellaneous databases

    EvolutionaryTracei P00634.
    PROi P00634.

    Gene expression databases

    Genevestigatori P00634.

    Family and domain databases

    Gene3Di 3.40.720.10. 1 hit.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR001952. Alkaline_phosphatase.
    IPR018299. Alkaline_phosphatase_AS.
    IPR017850. Alkaline_phosphatase_core.
    [Graphical view ]
    Pfami PF00245. Alk_phosphatase. 2 hits.
    [Graphical view ]
    PRINTSi PR00113. ALKPHPHTASE.
    SMARTi SM00098. alkPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00123. ALKALINE_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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).

    Entry informationi

    Entry nameiPPB_ECOLI
    AccessioniPrimary (citable) accession number: P00634
    Secondary accession number(s): P77801
    , P78051, Q2MC42, Q47041
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 162 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3