Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P74873

- SPTP_SALTY

UniProt

P74873 - SPTP_SALTY

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell

    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

    MLKYEERKLN NLTLSSFSKV GVSNDARLYI AKENTDKAYV APEKFSSKVL    50
    TWLGKMPLFK NTEVVQKHTE NIRVQDQKIL QTFLHALTEK YGETAVNDAL 100
    LMSRINMNKP LTQRLAVQIT ECVKAADEGF INLIKSKDNV GVRNAALVIK 150
    GGDTKVAEKN NDVGAESKQP LLDIALKGLK RTLPQLEQMD GNSLRENFQE 200
    MASGNGPLRS LMTNLQNLNK IPEAKQLNDY VTTLTNIQVG VARFSQWGTC 250
    GGEVERWVDK ASTHELTQAV KKIHVIAKEL KNVTAELEKI EAGAPMPQTM 300
    SGPTLGLARF AVSSIPINQQ TQVKLSDGMP VPVNTLTFDG KPVALAGSYP 350
    KNTPDALEAH MKMLLEKECS CLVVLTSEDQ MQAKQLPPYF RGSYTFGEVH 400
    TNSQKVSSAS QGEAIDQYNM QLSCGEKRYT IPVLHVKNWP DHQPLPSTDQ 450
    LEYLADRVKN SNQNGAPGRS SSDKHLPMIH CLGGVGRTGT MAAALVLKDN 500
    PHSNLEQVRA DFRDSRNNRM LEDASQFVQL KAMQAQLLMT TAS 543
    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

    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 1, 2014
    This is version 101 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