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Protein

Chaperone protein SigE

Gene

sigE

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone required for SopB/SigD stabilization and secretion.2 Publications

GO - Biological processi

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

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1099-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein SigE
Gene namesi
Name:sigE
Synonyms:pipC
Ordered Locus Names:STM1090
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014 Componenti: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 113113Chaperone protein SigEPRO_0000160575Add
BLAST

Proteomic databases

PaxDbiO30917.
PRIDEiO30917.

Expressioni

Inductioni

Transcriptionally regulated by InvF and SicA. Also regulated by SirA.

Interactioni

Subunit structurei

Homodimer or higher-order oligomers.

Protein-protein interaction databases

MINTiMINT-157122.
STRINGi99287.STM1090.

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 118Combined sources
Beta strandi24 – 263Combined sources
Beta strandi29 – 357Combined sources
Beta strandi37 – 4812Combined sources
Helixi53 – 6513Combined sources
Beta strandi66 – 727Combined sources
Beta strandi78 – 869Combined sources
Helixi91 – 11222Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K3SX-ray1.90A/B1-113[»]
ProteinModelPortaliO30917.
SMRiO30917. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO30917.

Family & Domainsi

Sequence similaritiesi

Belongs to the IpgE/SigE chaperone family.Curated

Phylogenomic databases

eggNOGiNOG67978.
HOGENOMiHOG000028304.
OMAiLMLEMCC.
OrthoDBiEOG6KT2RR.

Family and domain databases

InterProiIPR013095. T3SS_chaperone.
[Graphical view]
PfamiPF07824. Chaperone_III. 1 hit.
[Graphical view]
PIRSFiPIRSF034754. T3SS_chaperone. 1 hit.
ProDomiPD030752. T3SS_chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

O30917-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLLNRLYD ALGLDAPEDE PLLIIDDGIQ VYFNESDHTL EMCCPFMPLP
60 70 80 90 100
DDILTLQHFL RLNYTSAVTI GADADNTALV ALYRLPQTST EEEALTGFEL
110
FISNVKQLKE HYA
Length:113
Mass (Da):12,751
Last modified:January 1, 1998 - v1
Checksum:i34DEE3AB3944560E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021817 Genomic DNA. Translation: AAC46235.1.
AE006468 Genomic DNA. Translation: AAL20022.1.
RefSeqiNP_460063.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20022; AAL20022; STM1090.
GeneIDi1252608.
KEGGistm:STM1090.
PATRICi32380617. VBISalEnt20916_1154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021817 Genomic DNA. Translation: AAC46235.1.
AE006468 Genomic DNA. Translation: AAL20022.1.
RefSeqiNP_460063.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K3SX-ray1.90A/B1-113[»]
ProteinModelPortaliO30917.
SMRiO30917. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-157122.
STRINGi99287.STM1090.

Proteomic databases

PaxDbiO30917.
PRIDEiO30917.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20022; AAL20022; STM1090.
GeneIDi1252608.
KEGGistm:STM1090.
PATRICi32380617. VBISalEnt20916_1154.

Phylogenomic databases

eggNOGiNOG67978.
HOGENOMiHOG000028304.
OMAiLMLEMCC.
OrthoDBiEOG6KT2RR.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1099-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO30917.

Family and domain databases

InterProiIPR013095. T3SS_chaperone.
[Graphical view]
PfamiPF07824. Chaperone_III. 1 hit.
[Graphical view]
PIRSFiPIRSF034754. T3SS_chaperone. 1 hit.
ProDomiPD030752. T3SS_chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel Salmonella invasion locus homologous to Shigella ipgDE."
    Hong K.H., Miller V.L.
    J. Bacteriol. 180:1793-1802(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, REGULATION BY SIRA.
    Strain: ATCC 14028s / SGSG 2262.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "The putative invasion protein chaperone SicA acts together with InvF to activate the expression of Salmonella typhimurium virulence genes."
    Darwin K.H., Miller V.L.
    Mol. Microbiol. 35:949-960(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY INVF AND SICA.
    Strain: ATCC 14028s / SGSG 2262, LT2 and SL1344.
  4. "SigE is a chaperone for the Salmonella enterica serovar Typhimurium invasion protein SigD."
    Darwin K.H., Robinson L.S., Miller V.L.
    J. Bacteriol. 183:1452-1454(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: ATCC 14028s / SGSG 2262.
  5. "Structural and biochemical characterization of the type III secretion chaperones CesT and SigE."
    Luo Y., Bertero M.G., Frey E.A., Pfuetzner R.A., Wenk M.R., Creagh L., Marcus S.L., Lim D., Sicheri F., Kay C., Haynes C., Finlay B.B., Strynadka N.C.J.
    Nat. Struct. Biol. 8:1031-1036(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiSIGE_SALTY
AccessioniPrimary (citable) accession number: O30917
Secondary accession number(s): Q7CQS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 79 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

External Data

Dasty 3

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 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.