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O52787

- PTP_ACIJO

UniProt

O52787 - PTP_ACIJO

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Protein

Low molecular weight protein-tyrosine-phosphatase ptp

Gene

ptp

Organism
Acinetobacter johnsonii
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Dephosphorylates ptk. May be involved in the production and the transport of exopolysaccharides.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

Inhibited by ammonium molybdate, sodium orthovanadate, N-ethylmaleimide and iodoacetic acid.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101NucleophileBy similarity
Active sitei15 – 151By similarity
Active sitei115 – 1151Proton donorBy similarity

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Exopolysaccharide synthesis

Enzyme and pathway databases

UniPathwayiUPA00631.

Protein family/group databases

PptaseDBiP3D040495.

Names & Taxonomyi

Protein namesi
Recommended name:
Low molecular weight protein-tyrosine-phosphatase ptp (EC:3.1.3.48)
Gene namesi
Name:ptp
OrganismiAcinetobacter johnsonii
Taxonomic identifieri40214 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101C → S: Loss of activity. 1 Publication
Mutagenesisi16 – 161R → K: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 142142Low molecular weight protein-tyrosine-phosphatase ptpPRO_0000046566Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO52787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF7. PTHR11717:SF7. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.

Sequencei

Sequence statusi: Complete.

O52787-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQFKNILVVC IGNICRSPMA EYLLKQNYPQ LTIHSAGISG MIGYSADEKA
60 70 80 90 100
QLCMERIGID MSPHIAKKLN AELLKQADLI LVMSQNQQKH IEQTWPFAKG
110 120 130 140
KTFRLGHWQG KNIPDPYQHD QAFFDETSLL IQTCVADWTK HI
Length:142
Mass (Da):16,215
Last modified:June 1, 1998 - v1
Checksum:i62B53F3BDDBA5986
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y15162 Genomic DNA. Translation: CAA75430.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y15162 Genomic DNA. Translation: CAA75430.1 .

3D structure databases

ProteinModelPortali O52787.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

PptaseDBi P3D040495.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00631 .

Family and domain databases

InterProi IPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view ]
PANTHERi PTHR11717:SF7. PTHR11717:SF7. 1 hit.
Pfami PF01451. LMWPc. 1 hit.
[Graphical view ]
PRINTSi PR00719. LMWPTPASE.
SMARTi SM00226. LMWPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52788. SSF52788. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Characterization of a bacterial gene encoding an autophosphorylating protein tyrosine kinase."
    Grangeasse C., Doublet P., Vaganay E., Vincent C., Deleage G., Duclos B., Cozzone A.J.
    Gene 204:259-265(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Functional characterization of the low-molecular-mass phosphotyrosine-protein phosphatase of Acinetobacter johnsonii."
    Grangeasse C., Doublet P., Vincent C., Vaganay E., Riberty M., Duclos B., Cozzone A.J.
    J. Mol. Biol. 278:339-347(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-10 AND ARG-16.

Entry informationi

Entry nameiPTP_ACIJO
AccessioniPrimary (citable) accession number: O52787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 1998
Last modified: October 29, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3