Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8Y678 (STP1_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine phosphatase stp

EC=3.1.3.16
Gene names
Name:stp
Ordered Locus Names:lmo1821
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase that dephosphorylates EF-Tu. Ref.2

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions per subunit. Ref.2

Enzyme regulation

Activity not affected by inhibitors of phosphatases of the PPP family such as okadaic acid and cypermethrin, or by inhibitors of phosphatases of the PTP family such as sodium orthovanadate.

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein Ref.2.

Disruption phenotype

The stp-disrupted strain is 4 times less virulent than the wild strain, demonstrating that stp is required for full virulence of L.monocytogenes in BALB/c mice. Ref.2

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Biophysicochemical properties

Kinetic parameters:

KM=3.77 µM for MBP Ref.2

KM=0.62 µM for EF-Tu

Vmax=120.48 pmol/min/µg enzyme toward MBP

Vmax=2.94 pmol/min/µg enzyme toward EF-Tu

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Serine/threonine phosphatase stp
PRO_0000363063

Regions

Domain2 – 235234PP2C-like

Sites

Metal binding361Manganese 1 By similarity
Metal binding361Manganese 2 By similarity
Metal binding371Manganese 1; via carbonyl oxygen By similarity
Metal binding1941Manganese 2 By similarity
Metal binding2331Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Y678 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 47EE5DA232A43338

FASTA25228,026
        10         20         30         40         50         60 
MHAEFRTDRG RIRHHNEDNG GVFENKDNQP IVIVADGMGG HRAGDVASEM AVRLLSDAWK 

        70         80         90        100        110        120 
ETTALLTAEE IETWLRKTIQ EVNKEIVLYA ESEMDLNGMG TTLVAAIMAQ SQVVIANVGD 

       130        140        150        160        170        180 
SRGYLLQNHV LRQLTEDHSL VHELLRTGEI SKEDAMNHPR KNILLRALGV EGKVEVDTFV 

       190        200        210        220        230        240 
VPFQTSDTLL LCSDGLTNMV PETEMEEILK SKRTLSEKAD VFITKANSYG GEDNITVLLV 

       250 
ERDLTQKGRD AS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591981 Genomic DNA. Translation: CAC99899.1.
PIRAE1302.
RefSeqNP_465346.1. NC_003210.1.

3D structure databases

ProteinModelPortalQ8Y678.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo1821.

Protein family/group databases

PptaseDBP3D0611176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC99899; CAC99899; CAC99899.
GeneID985901.
KEGGlmo:lmo1821.
PATRIC20312835. VBILisMon69206_1866.

Organism-specific databases

GenoListLMO1821.

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000235782.
KOK01090.
OMAHEECQGM.
OrthoDBEOG65N17S.
PhylomeDBQ8Y678.

Enzyme and pathway databases

BioCycLMON169963:LMO1821-MONOMER.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSTP1_LISMO
AccessionPrimary (citable) accession number: Q8Y678
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families