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Protein

Transcriptional regulator SlyA

Gene

slyA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transcription regulator that can specifically activate or repress expression of target genes. Required for virulence and survival in the macrophage environment. Probably activates expression of ispA, xseB genes, and of omp operon.UniRule annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi49 – 7224H-T-H motifUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-HAMAP
  2. sequence-specific DNA binding transcription factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Virulence

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1454-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulator SlyAUniRule annotation
Alternative name(s):
Cytolysin SlyA
Salmolysin
Gene namesi
Name:slyAUniRule annotation
Ordered Locus Names:STM1444
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 144144Transcriptional regulator SlyAPRO_0000054393Add
BLAST

Proteomic databases

PRIDEiP40676.

Expressioni

Inductioni

During infection of the host cells. Down-regulated by itself. Activated by Mg2+ starvation in a phoP dependent manner.2 Publications

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-48666N.
STRINGi99287.STM1444.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2319Combined sources
Turni24 – 285Combined sources
Helixi31 – 4212Combined sources
Beta strandi45 – 484Combined sources
Helixi49 – 568Combined sources
Helixi60 – 7213Combined sources
Beta strandi75 – 784Combined sources
Beta strandi82 – 843Combined sources
Beta strandi89 – 924Combined sources
Helixi94 – 963Combined sources
Helixi97 – 11519Combined sources
Helixi120 – 13920Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DEUX-ray2.30A/B2-144[»]
3Q5FX-ray2.96A/B1-144[»]
3QPTX-ray2.40A1-144[»]
ProteinModelPortaliP40676.
SMRiP40676. Positions 1-140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 135134HTH marR-typeUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the SlyA family.UniRule annotation
Contains 1 HTH marR-type DNA-binding domain.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000221454.
KOiK06075.
OMAiTRHICAH.
OrthoDBiEOG6JMMVK.
PhylomeDBiP40676.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_01819. HTH_type_SlyA.
InterProiIPR000835. HTH_MarR-typ.
IPR023187. Tscrpt_reg_MarR-type_CS.
IPR023071. Tscrpt_reg_SlyA.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01047. MarR. 1 hit.
[Graphical view]
PRINTSiPR00598. HTHMARR.
SMARTiSM00347. HTH_MARR. 1 hit.
[Graphical view]
PROSITEiPS01117. HTH_MARR_1. 1 hit.
PS50995. HTH_MARR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESPLGSDLA RLVRIWRALI DHRLKPLELT QTHWVTLHNI HQLPPDQSQI
60 70 80 90 100
QLAKAIGIEQ PSLVRTLDQL EDKGLISRQT CASDRRAKRI KLTEKADALI
110 120 130 140
AEMEEVIHKT RGEILAGISS EEIELLIKLI AKLEHNIMEL HSHD
Length:144
Mass (Da):16,422
Last modified:October 24, 2003 - v3
Checksum:i2D37EB004F2D7439
GO

Sequence cautioni

The sequence AAA58796.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAL20366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 982DA → EP in AAA58796 (PubMed:8290552).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03842 Genomic DNA. Translation: AAA58796.1. Different initiation.
AE006468 Genomic DNA. Translation: AAL20366.1. Different initiation.
PIRiA36874.
RefSeqiNP_460407.2. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20366; AAL20366; STM1444.
GeneIDi1252962.
KEGGistm:STM1444.
PATRICi32381373. VBISalEnt20916_1527.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03842 Genomic DNA. Translation: AAA58796.1. Different initiation.
AE006468 Genomic DNA. Translation: AAL20366.1. Different initiation.
PIRiA36874.
RefSeqiNP_460407.2. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DEUX-ray2.30A/B2-144[»]
3Q5FX-ray2.96A/B1-144[»]
3QPTX-ray2.40A1-144[»]
ProteinModelPortaliP40676.
SMRiP40676. Positions 1-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48666N.
STRINGi99287.STM1444.

Proteomic databases

PRIDEiP40676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20366; AAL20366; STM1444.
GeneIDi1252962.
KEGGistm:STM1444.
PATRICi32381373. VBISalEnt20916_1527.

Phylogenomic databases

HOGENOMiHOG000221454.
KOiK06075.
OMAiTRHICAH.
OrthoDBiEOG6JMMVK.
PhylomeDBiP40676.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1454-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40676.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_01819. HTH_type_SlyA.
InterProiIPR000835. HTH_MarR-typ.
IPR023187. Tscrpt_reg_MarR-type_CS.
IPR023071. Tscrpt_reg_SlyA.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01047. MarR. 1 hit.
[Graphical view]
PRINTSiPR00598. HTHMARR.
SMARTiSM00347. HTH_MARR. 1 hit.
[Graphical view]
PROSITEiPS01117. HTH_MARR_1. 1 hit.
PS50995. HTH_MARR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 14028s / SGSG 2262.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "SlyA, a regulatory protein from Salmonella typhimurium, induces a haemolytic and pore-forming protein in Escherichia coli."
    Ludwig A., Tengel C., Bauer S., Bubert A., Benz R., Mollenkopf H.-J., Goebel W.
    Mol. Gen. Genet. 249:474-486(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Homologies between salmolysin and some bacterial regulatory proteins."
    Dehoux P., Cossart P.
    Mol. Microbiol. 15:591-591(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO MARR FAMILY.
  5. "SlyA, a transcriptional regulator of Salmonella typhimurium, is required for resistance to oxidative stress and is expressed in the intracellular environment of macrophages."
    Buchmeier N., Bossie S., Chen C.-Y., Fang F.C., Guiney D.G., Libby S.J.
    Infect. Immun. 65:3725-3730(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  6. "Interaction of the Salmonella typhimurium transcription and virulence factor SlyA with target DNA and identification of members of the SlyA regulon."
    Stapleton M.R., Norte V.A., Read R.C., Green J.
    J. Biol. Chem. 277:17630-17637(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION.
  7. "PhoP-responsive expression of the Salmonella enterica serovar typhimurium slyA gene."
    Norte V.A., Stapleton M.R., Green J.
    J. Bacteriol. 185:3508-3514(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiSLYA_SALTY
AccessioniPrimary (citable) accession number: P40676
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 24, 2003
Last modified: January 7, 2015
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be a toxin with hemolytic and cytolytic activity.1 Publication

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.