Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P74873

- SPTP_SALTY

UniProt

P74873 - SPTP_SALTY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Secreted effector protein SptP

Gene

sptP

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei481 – 4811Phosphocysteine intermediate

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Hydrolase, Protein phosphatase

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2895-MONOMER.

Protein family/group databases

PptaseDBiP3D0410147.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: 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

  1. extracellular space Source: InterPro
  2. host cell cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091R → A: Loss of GAP activity. 1 Publication
Mutagenesisi213 – 2131T → A: Loss of RAC1 binding and GAP activity. 1 Publication
Mutagenesisi246 – 2461Q → A: Loss of RAC1 binding and GAP activity. 1 Publication
Mutagenesisi249 – 2491T → A: Loss of RAC1 binding and GAP activity. 1 Publication
Mutagenesisi481 – 4811C → S: Loss of phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 543543Secreted effector protein SptPPRO_0000094866Add
BLAST

Proteomic databases

PaxDbiP74873.
PRIDEiP74873.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP74873. 2 interactions.
MINTiMINT-1535734.
STRINGi99287.STM2878.

Structurei

Secondary structure

1
543
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 545
Helixi62 – 7110
Helixi77 – 8913
Helixi93 – 10513
Helixi111 – 1133
Beta strandi116 – 1183
Helixi122 – 1276
Helixi130 – 1367
Helixi172 – 1809
Helixi183 – 1875
Helixi192 – 1943
Helixi198 – 2014
Helixi208 – 21811
Helixi222 – 2243
Helixi226 – 23510
Beta strandi239 – 2424
Helixi244 – 2463
Beta strandi250 – 2523
Helixi254 – 2585
Helixi263 – 28826
Turni312 – 3143
Beta strandi322 – 3243
Beta strandi330 – 3389
Beta strandi341 – 3477
Helixi354 – 36714
Beta strandi372 – 3743
Helixi378 – 3814
Turni382 – 3854
Turni389 – 3913
Beta strandi392 – 3965
Beta strandi399 – 4057
Helixi407 – 4093
Beta strandi415 – 42410
Beta strandi427 – 43610
Helixi448 – 45912
Beta strandi478 – 4858
Helixi486 – 49914
Helixi505 – 51511
Turni518 – 5214
Helixi524 – 53815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G4UX-ray2.30S161-543[»]
1G4WX-ray2.20R161-543[»]
1JYOX-ray1.90E/F35-139[»]
ProteinModelPortaliP74873.
SMRiP74873. Positions 36-139, 167-539.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP74873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 543264Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 139105Chaperone-bindingAdd
BLAST
Regioni167 – 290124GAPAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG74835.
HOGENOMiHOG000028733.
KOiK13740.
OMAiWIDKAST.
OrthoDBiEOG6423BT.

Family and domain databases

Gene3Di1.20.120.260. 1 hit.
3.90.190.10. 2 hits.
InterProiIPR011070. 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]
PfamiPF09119. SicP-binding. 1 hit.
PF00102. Y_phosphatase. 1 hit.
PF03545. YopE. 1 hit.
[Graphical view]
PRINTSiPR01371. BACYPHPHTASE.
SMARTiSM00194. PTPc. 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:
EMBL
GenBank
DDBJ
Links Updated
U63293 Genomic DNA. Translation: AAC44349.1.
AE006468 Genomic DNA. Translation: AAL21758.1.
RefSeqiNP_461799.1. NC_003197.1.
YP_005182747.1. NC_016810.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U63293 Genomic DNA. Translation: AAC44349.1 .
AE006468 Genomic DNA. Translation: AAL21758.1 .
RefSeqi NP_461799.1. NC_003197.1.
YP_005182747.1. NC_016810.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G4U X-ray 2.30 S 161-543 [» ]
1G4W X-ray 2.20 R 161-543 [» ]
1JYO X-ray 1.90 E/F 35-139 [» ]
ProteinModelPortali P74873.
SMRi P74873. Positions 36-139, 167-539.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P74873. 2 interactions.
MINTi MINT-1535734.
STRINGi 99287.STM2878.

Protein family/group databases

PptaseDBi P3D0410147.

Proteomic databases

PaxDbi P74873.
PRIDEi P74873.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL21758 ; AAL21758 ; STM2878 .
GeneIDi 1254401.
KEGGi stm:STM2878.
PATRICi 32384444. VBISalEnt20916_3034.

Phylogenomic databases

eggNOGi NOG74835.
HOGENOMi HOG000028733.
KOi K13740.
OMAi WIDKAST.
OrthoDBi EOG6423BT.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-2895-MONOMER.

Miscellaneous databases

EvolutionaryTracei P74873.

Family and domain databases

Gene3Di 1.20.120.260. 1 hit.
3.90.190.10. 2 hits.
InterProi IPR011070. 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 ]
Pfami PF09119. SicP-binding. 1 hit.
PF00102. Y_phosphatase. 1 hit.
PF03545. YopE. 1 hit.
[Graphical view ]
PRINTSi PR01371. BACYPHPHTASE.
SMARTi SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF47233. SSF47233. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF56568. SSF56568. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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: October 29, 2014
This is version 102 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

External Data

Dasty 3