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Protein

Low molecular weight protein-tyrosine-phosphatase Ptp

Gene

ptp

Organism
Acinetobacter johnsonii
Status
Reviewed-Annotation score: 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.

Pathway:iexopolysaccharide biosynthesis

This protein is involved in the pathway exopolysaccharide biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway exopolysaccharide biosynthesis and in Glycan metabolism.

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Exopolysaccharide synthesis

Enzyme and pathway databases

UniPathwayiUPA00631.

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.
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:
EMBLi
GenBanki
DDBJi
Links Updated
Y15162 Genomic DNA. Translation: CAA75430.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15162 Genomic DNA. Translation: CAA75430.1.

3D structure databases

ProteinModelPortaliO52787.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00631.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
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.
ProtoNetiSearch...

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: July 22, 2015
This is version 62 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.