Reviewed, UniProtKB/Swiss-Prot O52787 (PTP_ACIJO)

Names and origin

Protein names

Recommended name:
    Low molecular weight protein-tyrosine-phosphatase ptp
    EC=3.1.3.48

Gene names

Name:

ptp

Organism

Acinetobacter johnsonii

Taxonomic identifier

40214 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Dephosphorylates ptk. May be involved in the production and the transport of exopolysaccharides.
Catalytic activity	Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
Enzyme regulation	Inhibited by ammonium molybdate, sodium orthovanadate, N-ethylmaleimide and iodoacetic acid.
Pathway	Glycan metabolism; exopolysaccharide biosynthesis.
Sequence similarities	Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Ontologies

Keywords
Biological process	Exopolysaccharide synthesis
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 142	142	Low molecular weight protein-tyrosine-phosphatase ptp
Sites
	Active site	10	1	Nucleophile By similarity
	Active site	15	1	By similarity
	Active site	115	1	Proton donor By similarity
Experimental info
	Mutagenesis	10	1	C → S: Loss of activity
	Mutagenesis	16	1	R → K: Loss of activity

Sequences

	Sequence		Length	Mass (Da)
	O52787-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 62B53F3BDDBA5986	FASTA	142	16,215
	10 20 30 40 50 60 MQFKNILVVC IGNICRSPMA EYLLKQNYPQ LTIHSAGISG MIGYSADEKA QLCMERIGID 70 80 90 100 110 120 MSPHIAKKLN AELLKQADLI LVMSQNQQKH IEQTWPFAKG KTFRLGHWQG KNIPDPYQHD 130 140 QAFFDETSLL IQTCVADWTK HI

References

[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: 9434192] [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: 9571056] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-10 AND ARG-16.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y15162 Genomic DNA. Translation: CAA75430.1.
3D structure databases
HSSP	HSSP built from PDB template 1JL3 based on UniProtKB P45947.
ModBase	Search...
Protein family/group databases
PptaseDB	P3D040495.
Family and domain databases
InterPro	IPR000106. Tyr_Pase_low_mol_wt. [Graphical view]
PANTHER	PTHR11717. Low_mwt_PTPase. 1 hit.
Pfam	PF01451. LMWPc. 1 hit. [Graphical view]
PRINTS	PR00719. LMWPTPASE.
SMART	SM00226. LMWPc. 1 hit. [Graphical view]
ProDom	O52787. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

PTP_ACIJO

Accession

Primary (citable) accession number: O52787

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	June 1, 1998
Last modified:	July 22, 2008
This is version 37 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)