Q8Y678 (STP1_LISMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine phosphatase stp
EC=3.1.3.16

Gene names

Name:	stp
Ordered Locus Names:	lmo1821

Organism

Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]

Taxonomic identifier

169963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria monocytogenes

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase that dephosphorylates EF-Tu. Ref.2
Catalytic activity	A phosphoprotein + H2O = a protein + 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 component	Cytoplasm Membrane
Ligand	Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 252	252	Serine/threonine phosphatase stp		PRO_0000363063
Regions
	Domain	2 – 235	234	PP2C-like
Sites
	Metal binding	36	1	Manganese 1 By similarity
	Metal binding	36	1	Manganese 2 By similarity
	Metal binding	37	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	194	1	Manganese 2 By similarity
	Metal binding	233	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y678 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 47EE5DA232A43338	FASTA	252	28,026
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e.
[2]	"Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes." Archambaud C., Gouin E., Pizarro-Cerda J., Cossart P., Dussurget O. Mol. Microbiol. 56:383-396(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS PHOSPHATASE, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, IDENTIFICATION OF SUBSTRATE. Strain: ATCC BAA-679 / EGD-e.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591981 Genomic DNA. Translation: CAC99899.1.
PIR	AE1302.
RefSeq	NP_465346.1. NC_003210.1.
3D structure databases
ProteinModelPortal	Q8Y678.
ModBase	Search...
Protein-protein interaction databases
STRING	169963.lmo1821.
Protein family/group databases
PptaseDB	P3D0611176.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC99899; CAC99899; CAC99899.
GeneID	985901.
KEGG	lmo:lmo1821.
PATRIC	20312835. VBILisMon69206_1866.
Organism-specific databases
GenoList	LMO1821.
Phylogenomic databases
eggNOG	COG0631.
HOGENOM	HOG000235782.
KO	K01090.
OMA	VSHLGHN.
ProtClustDB	CLSK564625.
Family and domain databases
Gene3D	3.60.40.10. 1 hit.
InterPro	IPR001932. PP2C-like. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
ProtoNet	Search...

Entry information

Entry name

STP1_LISMO

Accession

Primary (citable) accession number: Q8Y678

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program