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P74873 (SPTP_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Secreted effector protein SptP

Including the following 2 domains:

  1. GTPase-activating protein
    Short name=GAP
  2. Tyrosine-protein phosphatase
    EC=3.1.3.48
Gene names
Name:sptP
Ordered Locus Names:STM2878
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein includes tyrosine phosphatase and GTPase activating protein (GAP) activities. After bacterial internalization, GAP mediates the reversal of the cytoskeletal changes induced by SopE. This function is independent of its tyrosine phosphatase activity, which remains unclear. Ref.1 Ref.4 Ref.5

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

The tyrosine phosphatase activity is inhibited by sodium vanadate. Ref.1

Subunit structure

Forms a complex with SicP. Binds host RAC1.

Subcellular location

Secreted. Host cytoplasm. Note: Secreted via type III secretion system 1 (SPI-1 TTSS), and delivered into the host cytoplasm. Ref.4

Miscellaneous

Requires SicP as a chaperone for its stability and for secretion. The structure of the SptP-SicP complex contains four molecules of the chaperone SicP, aligned in a linear fashion and arranged in two sets of tightly bound homodimers that bind two SptP molecules. The SicP homodimers do not interact with each other, but are held together by a molecular interface formed between two SptP molecules. The chaperone-binding domain of SptP does not adopt a globular fold for interaction with SicP. Each SptP molecule is wrapped around by three SicP chaperones (two chaperones from one homodimer and a third one from the opposite homodimer pair). SptP interacts with SicP chaperone dimers mainly through four regions of its chaperone-binding domain.

Sequence similarities

In the N-terminal section; belongs to the YopE family.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentHost cytoplasm
Secreted
   Molecular functionGTPase activation
Hydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: InterPro

host cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 543543Secreted effector protein SptP
PRO_0000094866

Regions

Domain280 – 543264Tyrosine-protein phosphatase
Region35 – 139105Chaperone-binding
Region167 – 290124GAP

Sites

Active site4811Phosphocysteine intermediate

Experimental info

Mutagenesis2091R → A: Loss of GAP activity. Ref.4
Mutagenesis2131T → A: Loss of RAC1 binding and GAP activity. Ref.5
Mutagenesis2461Q → A: Loss of RAC1 binding and GAP activity. Ref.5
Mutagenesis2491T → A: Loss of RAC1 binding and GAP activity. Ref.5
Mutagenesis4811C → S: Loss of phosphatase activity. Ref.1

Secondary structure

.............................................................................. 543
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P74873 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 060D2113EB5B5429

FASTA54360,048
        10         20         30         40         50         60 
MLKYEERKLN NLTLSSFSKV GVSNDARLYI AKENTDKAYV APEKFSSKVL TWLGKMPLFK 

        70         80         90        100        110        120 
NTEVVQKHTE NIRVQDQKIL QTFLHALTEK YGETAVNDAL LMSRINMNKP LTQRLAVQIT 

       130        140        150        160        170        180 
ECVKAADEGF INLIKSKDNV GVRNAALVIK GGDTKVAEKN NDVGAESKQP LLDIALKGLK 

       190        200        210        220        230        240 
RTLPQLEQMD GNSLRENFQE MASGNGPLRS LMTNLQNLNK IPEAKQLNDY VTTLTNIQVG 

       250        260        270        280        290        300 
VARFSQWGTC GGEVERWVDK ASTHELTQAV KKIHVIAKEL KNVTAELEKI EAGAPMPQTM 

       310        320        330        340        350        360 
SGPTLGLARF AVSSIPINQQ TQVKLSDGMP VPVNTLTFDG KPVALAGSYP KNTPDALEAH 

       370        380        390        400        410        420 
MKMLLEKECS CLVVLTSEDQ MQAKQLPPYF RGSYTFGEVH TNSQKVSSAS QGEAIDQYNM 

       430        440        450        460        470        480 
QLSCGEKRYT IPVLHVKNWP DHQPLPSTDQ LEYLADRVKN SNQNGAPGRS SSDKHLPMIH 

       490        500        510        520        530        540 
CLGGVGRTGT MAAALVLKDN PHSNLEQVRA DFRDSRNNRM LEDASQFVQL KAMQAQLLMT 


TAS 

« Hide

References

« Hide 'large scale' references
[1]"A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium."
Kaniga K., Uralil J., Bliska J.B., Galan J.E.
Mol. Microbiol. 21:633-641(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME REGULATION, FUNCTION, MUTAGENESIS OF CYS-481.
Strain: SL1344.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Identification of a specific chaperone for SptP, a substrate of the centisome 63 type III secretion system of Salmonella typhimurium."
Fu Y., Galan J.E.
J. Bacteriol. 180:3393-3399(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SICP.
Strain: SL1344.
[4]"A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion."
Fu Y., Galan J.E.
Nature 401:293-297(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-209.
Strain: SB300.
[5]"Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1."
Stebbins C.E., Galan J.E.
Mol. Cell 6:1449-1460(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 161-543 IN COMPLEX WITH RAC1, FUNCTION, MUTAGENESIS OF THR-213; GLN-246 AND THR-249.
[6]"Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion."
Stebbins C.E., Galan J.E.
Nature 414:77-81(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 35-139 IN COMPLEX WITH SICP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U63293 Genomic DNA. Translation: AAC44349.1.
AE006468 Genomic DNA. Translation: AAL21758.1.
RefSeqNP_461799.1. NC_003197.1.
YP_005182747.1. NC_016810.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G4UX-ray2.30S161-543[»]
1G4WX-ray2.20R161-543[»]
1JYOX-ray1.90E/F35-139[»]
ProteinModelPortalP74873.
SMRP74873. Positions 36-139, 167-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP74873. 2 interactions.
MINTMINT-1535734.
STRING99287.STM2878.

Protein family/group databases

PptaseDBP3D0410147.

Proteomic databases

PaxDbP74873.
PRIDEP74873.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL21758; AAL21758; STM2878.
GeneID1254401.
KEGGstm:STM2878.
PATRIC32384444. VBISalEnt20916_3034.

Phylogenomic databases

eggNOGNOG74835.
HOGENOMHOG000028733.
KOK13740.
OMAWIDKAST.
OrthoDBEOG6423BT.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2895-MONOMER.

Family and domain databases

Gene3D1.20.120.260. 1 hit.
3.90.190.10. 2 hits.
InterProIPR011070. Globular_prot_asu/bsu.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR015203. SicP-binding.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR003546. Tyr_Pase_SptP/YopH.
IPR014773. Uncharacterised_dom_YopE.
[Graphical view]
PfamPF09119. SicP-binding. 1 hit.
PF00102. Y_phosphatase. 1 hit.
PF03545. YopE. 1 hit.
[Graphical view]
PRINTSPR01371. BACYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF47233. SSF47233. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF56568. SSF56568. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP74873.

Entry information

Entry nameSPTP_SALTY
AccessionPrimary (citable) accession number: P74873
Secondary accession number(s): Q7CPX3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: February 1, 1997
Last modified: June 11, 2014
This is version 100 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references