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Protein

Secreted effector protein SifA

Gene

sifA

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 is required for endosomal tubulation and formation of Salmonella-induced filaments (Sifs), which are filamentous structures containing lysosomal membrane glycoproteins within epithelial cells. Sif formation is concomitant with intracellular bacterial replication.3 Publications

GO - Biological processi

  • pathogenesis Source: UniProtKB-KW
  • regulation of protein localization Source: AgBase
Complete GO annotation...

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1233-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Secreted effector protein SifA
Gene namesi
Name:sifA
Ordered Locus Names:STM1224
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

  • Secreted
  • Host cytoplasm
  • Host cell membrane

  • Note: Secreted via type III secretion system 2 (SPI-2 TTSS), and delivered into the host cytoplasm. It associates with membranes and colocalizes with microtubules along the length of Sifs in infected cells.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host membrane, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene do not produce Sifs in epithelial cells and show attenuated virulence in mice.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1301L → D: Loss of interaction with host PLEKHM2. Fails to induce host endosomal tubulation; when associated with D-131. 1 Publication
Mutagenesisi131 – 1311M → D: Alters interaction with host PLEKHM2. Fails to induce host endosomal tubulation; when associated with D-130. 1 Publication
Mutagenesisi197 – 1971W → A: Fails to induce host endosomal tubulation; when associated with A-201. 1 Publication
Mutagenesisi201 – 2011E → A: Fails to induce host endosomal tubulation; when associated with A-197. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Secreted effector protein SifAPRO_0000097760Add
BLAST

Proteomic databases

PaxDbiQ56061.
PRIDEiQ56061.

Interactioni

Subunit structurei

Interacts with host PLEKHM2. Interacts with SseJ; the interaction is indirect.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PLEKHM2Q8IWE53EBI-10765408,EBI-726484From a different organism.

Protein-protein interaction databases

DIPiDIP-46411N.
IntActiQ56061. 2 interactions.
STRINGi99287.STM1224.

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 3410Combined sources
Helixi35 – 373Combined sources
Helixi42 – 5413Combined sources
Beta strandi55 – 584Combined sources
Helixi62 – 7514Combined sources
Helixi78 – 814Combined sources
Beta strandi84 – 874Combined sources
Helixi89 – 913Combined sources
Beta strandi96 – 1016Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi126 – 1327Combined sources
Beta strandi145 – 1539Combined sources
Turni154 – 1574Combined sources
Beta strandi158 – 16710Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi174 – 1774Combined sources
Helixi180 – 1878Combined sources
Beta strandi190 – 1923Combined sources
Turni194 – 1963Combined sources
Helixi197 – 22024Combined sources
Turni221 – 2233Combined sources
Helixi228 – 24114Combined sources
Helixi258 – 26710Combined sources
Turni270 – 2723Combined sources
Helixi273 – 2764Combined sources
Helixi283 – 30321Combined sources
Helixi307 – 32418Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CXBX-ray2.60A1-336[»]
3HW2X-ray3.30A1-336[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56061.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 330330Interaction with host PLEKHM2Add
BLAST

Domaini

Domains throughout the protein, and not only the N-terminus, are required for secretion and translocation. Both N- and C-terminal domains are also required for formation of tubules.1 Publication

Sequence similaritiesi

Belongs to the Sif family.Curated

Phylogenomic databases

HOGENOMiHOG000028279.
KOiK15347.
OMAiLETMTMC.

Family and domain databases

InterProiIPR010637. Sif.
[Graphical view]
PfamiPF06767. Sif. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q56061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPITIGNGFL KSEILTNSPR NTKEAWWKVL WEKIKDFFFS TGKAKADRCL
60 70 80 90 100
HEMLFAERAP TRERLTEIFF ELKELACASQ RDRFQVHNPH ENDATIILRI
110 120 130 140 150
MDQNEENELL RITQNTDTFS CEVMGNLYFL MKDRPDILKS HPQMTAMIKR
160 170 180 190 200
RYSEIVDYPL PSTLCLNPAG APILSVPLDN IEGYLYTELR KGHLDGWKAQ
210 220 230 240 250
EKATYLAAKI QSGIEKTTRI LHHANISEST QQNAFLETMA MCGLKQLEIP
260 270 280 290 300
PPHTHIPIEK MVKEVLLADK TFQAFLVTDP STSQSMLAEI VEAISDQVFH
310 320 330
AIFRIDPQAI QKMAEEQLTT LHVRSEQQSG CLCCFL
Length:336
Mass (Da):38,498
Last modified:November 1, 1997 - v1
Checksum:i83C6185148A774B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51867 Genomic DNA. Translation: AAA97467.1.
AE006468 Genomic DNA. Translation: AAL20153.1.
PIRiS71033.
RefSeqiNP_460194.1. NC_003197.1.
WP_001520468.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20153; AAL20153; STM1224.
GeneIDi1252742.
KEGGistm:STM1224.
PATRICi32380899. VBISalEnt20916_1294.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51867 Genomic DNA. Translation: AAA97467.1.
AE006468 Genomic DNA. Translation: AAL20153.1.
PIRiS71033.
RefSeqiNP_460194.1. NC_003197.1.
WP_001520468.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CXBX-ray2.60A1-336[»]
3HW2X-ray3.30A1-336[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46411N.
IntActiQ56061. 2 interactions.
STRINGi99287.STM1224.

Proteomic databases

PaxDbiQ56061.
PRIDEiQ56061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20153; AAL20153; STM1224.
GeneIDi1252742.
KEGGistm:STM1224.
PATRICi32380899. VBISalEnt20916_1294.

Phylogenomic databases

HOGENOMiHOG000028279.
KOiK15347.
OMAiLETMTMC.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1233-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ56061.

Family and domain databases

InterProiIPR010637. Sif.
[Graphical view]
PfamiPF06767. Sif. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSIFA_SALTY
AccessioniPrimary (citable) accession number: Q56061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.