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Protein

Secreted effector protein SptP

Gene

sptP

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei481Phosphocysteine intermediate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Hydrolase, Protein phosphatase

Keywords - Biological processi

Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Secreted effector protein SptP
Including the following 2 domains:
GTPase-activating protein
Short name:
GAP
Tyrosine-protein phosphatase (EC:3.1.3.48)
Gene namesi
Name:sptP
Ordered Locus Names:STM2878
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

  • Secreted 1 Publication
  • Host cytoplasm 1 Publication

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi209R → A: Loss of GAP activity. 1 Publication1
Mutagenesisi213T → A: Loss of RAC1 binding and GAP activity. 1 Publication1
Mutagenesisi246Q → A: Loss of RAC1 binding and GAP activity. 1 Publication1
Mutagenesisi249T → A: Loss of RAC1 binding and GAP activity. 1 Publication1
Mutagenesisi481C → S: Loss of phosphatase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000948661 – 543Secreted effector protein SptPAdd BLAST543

Proteomic databases

PaxDbiP74873.
PRIDEiP74873.

Interactioni

Subunit structurei

Forms a complex with SicP. Binds host RAC1.2 Publications

Protein-protein interaction databases

IntActiP74873. 3 interactors.
MINTiMINT-1535734.
STRINGi99287.STM2878.

Structurei

Secondary structure

1543
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 54Combined sources5
Helixi62 – 71Combined sources10
Helixi77 – 89Combined sources13
Helixi93 – 105Combined sources13
Helixi111 – 113Combined sources3
Beta strandi116 – 118Combined sources3
Helixi122 – 127Combined sources6
Helixi130 – 136Combined sources7
Helixi172 – 180Combined sources9
Helixi183 – 187Combined sources5
Helixi192 – 194Combined sources3
Helixi198 – 201Combined sources4
Helixi208 – 218Combined sources11
Helixi222 – 224Combined sources3
Helixi226 – 235Combined sources10
Beta strandi239 – 242Combined sources4
Helixi244 – 246Combined sources3
Beta strandi250 – 252Combined sources3
Helixi254 – 258Combined sources5
Helixi263 – 288Combined sources26
Turni312 – 314Combined sources3
Beta strandi322 – 324Combined sources3
Beta strandi330 – 338Combined sources9
Beta strandi341 – 347Combined sources7
Helixi354 – 367Combined sources14
Beta strandi372 – 374Combined sources3
Helixi378 – 381Combined sources4
Turni382 – 385Combined sources4
Turni389 – 391Combined sources3
Beta strandi392 – 396Combined sources5
Beta strandi399 – 405Combined sources7
Helixi407 – 409Combined sources3
Beta strandi415 – 424Combined sources10
Beta strandi427 – 436Combined sources10
Helixi448 – 459Combined sources12
Beta strandi478 – 485Combined sources8
Helixi486 – 499Combined sources14
Helixi505 – 515Combined sources11
Turni518 – 521Combined sources4
Helixi524 – 538Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G4UX-ray2.30S161-543[»]
1G4WX-ray2.20R161-543[»]
1JYOX-ray1.90E/F35-139[»]
ProteinModelPortaliP74873.
SMRiP74873.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP74873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini280 – 543Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST264

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 139Chaperone-bindingAdd BLAST105
Regioni167 – 290GAPAdd BLAST124

Sequence similaritiesi

In the N-terminal section; belongs to the YopE family.Curated
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410641W. Bacteria.
ENOG4112D26. LUCA.
HOGENOMiHOG000028733.
KOiK13740.
OMAiWIDKAST.

Family and domain databases

CDDicd00219. ToxGAP. 1 hit.
Gene3Di1.20.120.260. 1 hit.
3.90.190.10. 2 hits.
InterProiIPR011070. Globular_prot_asu/bsu.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR015203. SicP-binding.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR003546. Tyr_Pase_SptP/YopH.
IPR000387. TYR_PHOSPHATASE_dom.
IPR014773. Uncharacterised_dom_YopE.
[Graphical view]
PfamiPF09119. SicP-binding. 1 hit.
PF00102. Y_phosphatase. 1 hit.
PF03545. YopE. 1 hit.
[Graphical view]
PRINTSiPR01371. BACYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF47233. SSF47233. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF56568. SSF56568. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P74873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKYEERKLN NLTLSSFSKV GVSNDARLYI AKENTDKAYV APEKFSSKVL
60 70 80 90 100
TWLGKMPLFK NTEVVQKHTE NIRVQDQKIL QTFLHALTEK YGETAVNDAL
110 120 130 140 150
LMSRINMNKP LTQRLAVQIT ECVKAADEGF INLIKSKDNV GVRNAALVIK
160 170 180 190 200
GGDTKVAEKN NDVGAESKQP LLDIALKGLK RTLPQLEQMD GNSLRENFQE
210 220 230 240 250
MASGNGPLRS LMTNLQNLNK IPEAKQLNDY VTTLTNIQVG VARFSQWGTC
260 270 280 290 300
GGEVERWVDK ASTHELTQAV KKIHVIAKEL KNVTAELEKI EAGAPMPQTM
310 320 330 340 350
SGPTLGLARF AVSSIPINQQ TQVKLSDGMP VPVNTLTFDG KPVALAGSYP
360 370 380 390 400
KNTPDALEAH MKMLLEKECS CLVVLTSEDQ MQAKQLPPYF RGSYTFGEVH
410 420 430 440 450
TNSQKVSSAS QGEAIDQYNM QLSCGEKRYT IPVLHVKNWP DHQPLPSTDQ
460 470 480 490 500
LEYLADRVKN SNQNGAPGRS SSDKHLPMIH CLGGVGRTGT MAAALVLKDN
510 520 530 540
PHSNLEQVRA DFRDSRNNRM LEDASQFVQL KAMQAQLLMT TAS
Length:543
Mass (Da):60,048
Last modified:February 1, 1997 - v1
Checksum:i060D2113EB5B5429
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63293 Genomic DNA. Translation: AAC44349.1.
AE006468 Genomic DNA. Translation: AAL21758.1.
RefSeqiNP_461799.1. NC_003197.1.
WP_000922300.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21758; AAL21758; STM2878.
GeneIDi1254401.
KEGGistm:STM2878.
PATRICi32384444. VBISalEnt20916_3034.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63293 Genomic DNA. Translation: AAC44349.1.
AE006468 Genomic DNA. Translation: AAL21758.1.
RefSeqiNP_461799.1. NC_003197.1.
WP_000922300.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G4UX-ray2.30S161-543[»]
1G4WX-ray2.20R161-543[»]
1JYOX-ray1.90E/F35-139[»]
ProteinModelPortaliP74873.
SMRiP74873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP74873. 3 interactors.
MINTiMINT-1535734.
STRINGi99287.STM2878.

Proteomic databases

PaxDbiP74873.
PRIDEiP74873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21758; AAL21758; STM2878.
GeneIDi1254401.
KEGGistm:STM2878.
PATRICi32384444. VBISalEnt20916_3034.

Phylogenomic databases

eggNOGiENOG410641W. Bacteria.
ENOG4112D26. LUCA.
HOGENOMiHOG000028733.
KOiK13740.
OMAiWIDKAST.

Miscellaneous databases

EvolutionaryTraceiP74873.

Family and domain databases

CDDicd00219. ToxGAP. 1 hit.
Gene3Di1.20.120.260. 1 hit.
3.90.190.10. 2 hits.
InterProiIPR011070. Globular_prot_asu/bsu.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR015203. SicP-binding.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR003546. Tyr_Pase_SptP/YopH.
IPR000387. TYR_PHOSPHATASE_dom.
IPR014773. Uncharacterised_dom_YopE.
[Graphical view]
PfamiPF09119. SicP-binding. 1 hit.
PF00102. Y_phosphatase. 1 hit.
PF03545. YopE. 1 hit.
[Graphical view]
PRINTSiPR01371. BACYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF47233. SSF47233. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF56568. SSF56568. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPTP_SALTY
AccessioniPrimary (citable) accession number: P74873
Secondary accession number(s): Q7CPX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.