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O30917 (SIGE_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chaperone protein SigE
Gene names
Name:sigE
Synonyms:pipC
Ordered Locus Names:STM1090
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length113 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Molecular chaperone required for SopB/SigD stabilization and secretion. Ref.1 Ref.4

Subunit structure

Homodimer or higher-order oligomers.

Subcellular location

Cytoplasm Probable.

Induction

Transcriptionally regulated by InvF and SicA. Also regulated by SirA. Ref.1 Ref.3

Sequence similarities

Belongs to the IpgE/SigE chaperone family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentCytoplasm
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 113113Chaperone protein SigE
PRO_0000160575

Secondary structure

................ 113
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O30917 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 34DEE3AB3944560E

FASTA11312,751
        10         20         30         40         50         60 
MESLLNRLYD ALGLDAPEDE PLLIIDDGIQ VYFNESDHTL EMCCPFMPLP DDILTLQHFL 

        70         80         90        100        110 
RLNYTSAVTI GADADNTALV ALYRLPQTST EEEALTGFEL FISNVKQLKE HYA 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel Salmonella invasion locus homologous to Shigella ipgDE."
Hong K.H., Miller V.L.
J. Bacteriol. 180:1793-1802(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, REGULATION BY SIRA.
Strain: ATCC 14028s / SGSG 2262.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
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(2000) [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(2001) [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(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF021817 Genomic DNA. Translation: AAC46235.1.
AE006468 Genomic DNA. Translation: AAL20022.1.
RefSeqNP_460063.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K3SX-ray1.90A/B1-113[»]
ProteinModelPortalO30917.
SMRO30917. Positions 1-113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-157122.
STRING99287.STM1090.

Proteomic databases

PaxDbO30917.
PRIDEO30917.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20022; AAL20022; STM1090.
GeneID1252608.
KEGGstm:STM1090.
PATRIC32380617. VBISalEnt20916_1154.

Phylogenomic databases

eggNOGNOG67978.
HOGENOMHOG000028304.
OMALMLEMCC.
OrthoDBEOG6KT2RR.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1099-MONOMER.

Family and domain databases

InterProIPR013095. T3SS_chaperone.
[Graphical view]
PfamPF07824. Chaperone_III. 1 hit.
[Graphical view]
PIRSFPIRSF034754. T3SS_chaperone. 1 hit.
ProDomPD030752. T3SS_chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceO30917.

Entry information

Entry nameSIGE_SALTY
AccessionPrimary (citable) accession number: O30917
Secondary accession number(s): Q7CQS7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references