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Protein

Guanine nucleotide exchange factor SopE

Gene

sopE

Organism
Salmonella typhimurium
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Activator for both CDC42 and RAC1 by directly engaging these Rho GTPases and acting as potent guanine nucleotide exchange factor (GEF). This activation results in actin cytoskeleton rearrangements and stimulates membrane ruffling, promoting bacterial entry into non-phagocytic cells. Also activates MAPK8, indicating that it is capable of stimulating signaling pathways that can lead to nuclear responses. Chaperone InvB is required for secretion and translocation of SopE.2 Publications

Miscellaneous

Encoded within a prophage region, which is only present in very few Salmonella isolates. SopE-expressing S.typhimurium strains are associated with severe epidemics.

Caution

SopE is not present in the complete genome strain LT2.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei103Helps stabilization of SopE-CDC421
Sitei109Helps stabilization of SopE-CDC421
Sitei124Helps stabilization of SopE-CDC421
Sitei131Helps stabilization of SopE-CDC421
Sitei174Helps stabilization of SopE-CDC421
Sitei194Helps stabilization of SopE-CDC421
Sitei198Helps stabilization of SopE-CDC421

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGTPase activation, Guanine-nucleotide releasing factor
Biological processVirulence

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide exchange factor SopE
Alternative name(s):
Effector protein SopE
Toxin SopE
Gene namesi
Name:sopE
OrganismiSalmonella typhimurium
Taxonomic identifieri90371 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103D → A: 4-fold reduction in GEF activity. 1 Publication1
Mutagenesisi103D → E: 2-fold reduction in GEF activity. 1 Publication1
Mutagenesisi109Q → A: 700-fold reduction in GEF activity. 1 Publication1
Mutagenesisi109Q → N: 160-fold reduction in GEF activity. 1 Publication1
Mutagenesisi124D → A or E: 160-800-fold reduction in GEF activity. 1 Publication1
Mutagenesisi168G → A: 5000-fold reduction in GEF activity. 1 Publication1
Mutagenesisi168G → V: 20000-fold reduction in GEF activity. 1 Publication1
Mutagenesisi168Missing : 800-fold reduction in GEF activity. 1 Publication1
Mutagenesisi198K → A or R: No effect. 1 Publication1
Mutagenesisi198K → E: More than 20-fold reduction in GEF activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002207402 – 240Guanine nucleotide exchange factor SopEAdd BLAST239

Expressioni

Inductioni

Transcriptionally activated by InvF in association with SicA.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P609532EBI-602254,EBI-81752From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

IntActiO52623, 1 interactor

Structurei

Secondary structure

1240
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi80 – 94Combined sources15
Helixi96 – 102Combined sources7
Helixi104 – 132Combined sources29
Helixi138 – 150Combined sources13
Beta strandi155 – 158Combined sources4
Beta strandi161 – 164Combined sources4
Helixi173 – 183Combined sources11
Helixi185 – 188Combined sources4
Helixi191 – 209Combined sources19
Helixi210 – 213Combined sources4
Helixi221 – 236Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GZSX-ray2.30B/D78-240[»]
ProteinModelPortaliO52623
SMRiO52623
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO52623

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni15 – 78Interaction with InvBAdd BLAST64
Regioni78 – 240GEF catalytic domainAdd BLAST163
Regioni165 – 172Catalytic loop involved in contact with CDC428
Regioni166 – 169Core-loop involved in conformational changes in complex with CDC424

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.4120.10, 1 hit
InterProiView protein in InterPro
IPR005414 SopE
IPR035949 SopE-like_GEF_dom_sf
IPR016019 SopE_GEF_dom
IPR016018 SopE_N_dom
PfamiView protein in Pfam
PF05364 SecIII_SopE_N, 1 hit
PF07487 SopE_GEF, 1 hit
PIRSFiPIRSF034781 SecIII_sopE, 1 hit
PRINTSiPR01593 SOPEPROTEIN
SUPFAMiSSF81832 SSF81832, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O52623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKITLSPQN FRIQKQETTL LKEKSTEKNS LAKSILAVKN HFIELRSKLS
60 70 80 90 100
ERFISHKNTE SSATHFHRGS ASEGRAVLTN KVVKDFMLQT LNDIDIRGSA
110 120 130 140 150
SKDPAYASQT REAILSAVYS KNKDQCCNLL ISKGINIAPF LQEIGEAAKN
160 170 180 190 200
AGLPGTTKND VFTPSGAGAN PFITPLISSA NSKYPRMFIN QHQQASFKIY
210 220 230 240
AEKIIMTEVA PLFNECAMPT PQQFQLILEN IANKYIQNTP
Length:240
Mass (Da):26,636
Last modified:January 23, 2007 - v3
Checksum:iF636F6C437018D03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043239 Genomic DNA Translation: AAC02071.1
RefSeqiWP_000161707.1, NZ_PHIR01000016.1

Genome annotation databases

PATRICifig|90371.1188.peg.2871

Similar proteinsi

Entry informationi

Entry nameiSOPE_SALTM
AccessioniPrimary (citable) accession number: O52623
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 89 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
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Main funding by: National Institutes of Health