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P0A0J0 (SIGA_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:
RNA polymerase sigma factor SigA
Gene names
Name:sigA
Synonyms:plaC, rpoD
Ordered Locus Names:SAOUHSC_01662
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. Ref.3

Subunit structure

Interacts transiently with the RNA polymerase catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNA polymerase holoenzyme that can initiate transcription By similarity. Interacts (via sigma-70 factor domain 4) with the phage G1 protein gp67; this inhibits rRNA synthesis. Interaction with phage G1 protein gp67 does not inhibit transcription in general, but selectively inhibits transcription from promoters that require interaction of the RNA polymerase alpha subunit with DNA sequences upstream of the -35 promoter element. Ref.3

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00963.

Domain

Contains 4 domains, connected by flexible linkers. In the active conformation, the domains are in an extended conformation, each making extensive interactions with the RNA polymerase catalytic core By similarity. HAMAP-Rule MF_00963

In the autoinhibited state, sigma-70 factor domain-1 packs closely together with sigma-70 factor domains-2 and -4, contrary to the extended conformation that is seen when the protein is part of the RNA polymerase holoenzyme By similarity. HAMAP-Rule MF_00963

The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC By similarity. HAMAP-Rule MF_00963

The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-sigma factors prevents interaction of sigma factors with the RNA polymerase catalytic core By similarity. HAMAP-Rule MF_00963

Sequence similarities

Belongs to the sigma-70 factor family. RpoD/SigA subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368RNA polymerase sigma factor SigA HAMAP-Rule MF_00963
PRO_0000093916

Regions

DNA binding329 – 34820H-T-H motif By similarity
Region16 – 9075Sigma-70 factor domain-1 HAMAP-Rule MF_00963
Region135 – 20571Sigma-70 factor domain-2 HAMAP-Rule MF_00963
Region214 – 29178Sigma-70 factor domain-3 HAMAP-Rule MF_00963
Region303 – 35654Sigma-70 factor domain-4 HAMAP-Rule MF_00963
Motif159 – 1624Interaction with polymerase core subunit RpoC HAMAP-Rule MF_00963

Natural variations

Natural variant2091P → S in plaC1 mutation; results in a narrower specificity for promoters.

Secondary structure

.......... 368
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A0J0 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: AB029CA4F5A93A55

FASTA36842,171
        10         20         30         40         50         60 
MSDNTVKIKK QTIDPTLTLE DVKKQLIEKG KKEGHLSHEE IAEKLQNFDI DSDQMDDFFD 

        70         80         90        100        110        120 
QLNDNDISLV NEKDSSDTDE KLNPSDLSAP PGVKINDPVR MYLKEIGRVN LLSAQEEIEL 

       130        140        150        160        170        180 
AKRIEQGDEV AKSRLAEANL RLVVSIAKRY VGRGMLFLDL IQEGNMGLIK AVEKFDFNKG 

       190        200        210        220        230        240 
FKFSTYATWW IRQAITRAIA DQARTIRIPV HMVETINKLI RVQRQLLQDL GRDPAPEEIG 

       250        260        270        280        290        300 
EEMDLPAEKV REILKIAQEP VSLETPIGEE DDSHLGDFIE DQEAQSPSDH AAYELLKEQL 

       310        320        330        340        350        360 
EDVLDTLTDR EENVLRLRFG LDDGRTRTLE EVGKVFGVTR ERIRQIEAKA LRKLRHPSRS 


KRLKDFMD 

« Hide

References

« Hide 'large scale' references
[1]"The Staphylococcus aureus chromosomal gene plaC, identified by mutations amplifying plasmid pT181, encodes a sigma factor."
Basheer R., Iordanescu S.
Nucleic Acids Res. 19:4921-4924(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.
[3]"Promoter-specific transcription inhibition in Staphylococcus aureus by a phage protein."
Osmundson J., Montero-Diez C., Westblade L.F., Hochschild A., Darst S.A.
Cell 151:1005-1016(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 297-368 IN COMPLEX WITH PHAGE PROTEIN GP67, FUNCTION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63177 Genomic DNA. Translation: AAB59090.1.
CP000253 Genomic DNA. Translation: ABD30737.1.
PIRS34442.
RefSeqYP_500173.1. NC_007795.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4G6DX-ray2.00A297-368[»]
4G8XX-ray3.00A/C296-357[»]
4G94X-ray2.00A297-357[»]
ProteinModelPortalP0A0J0.
SMRP0A0J0. Positions 38-368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_01662.

Proteomic databases

PRIDEP0A0J0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD30737; ABD30737; SAOUHSC_01662.
GeneID3920074.
KEGGsao:SAOUHSC_01662.
PATRIC19580705. VBIStaAur99865_1512.

Phylogenomic databases

eggNOGCOG0568.
HOGENOMHOG000270273.
KOK03086.
OMAITNRESQ.
OrthoDBEOG6XHC70.
ProtClustDBPRK09210.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-1587-MONOMER.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
HAMAPMF_00963. Sigma70_RpoD_SigA.
InterProIPR014284. RNA_pol_sigma-70_dom.
IPR000943. RNA_pol_sigma70.
IPR009042. RNA_pol_sigma70_r1_2.
IPR007627. RNA_pol_sigma70_r2.
IPR007624. RNA_pol_sigma70_r3.
IPR007630. RNA_pol_sigma70_r4.
IPR007127. RNA_pol_sigma_70_r1_1.
IPR013325. RNA_pol_sigma_r2.
IPR013324. RNA_pol_sigma_r3_r4.
IPR012760. RNA_pol_sigma_RpoD_C.
IPR028630. Sigma70_RpoD.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF03979. Sigma70_r1_1. 1 hit.
PF00140. Sigma70_r1_2. 1 hit.
PF04542. Sigma70_r2. 1 hit.
PF04539. Sigma70_r3. 1 hit.
PF04545. Sigma70_r4. 1 hit.
[Graphical view]
PRINTSPR00046. SIGMA70FCT.
SUPFAMSSF88659. SSF88659. 2 hits.
SSF88946. SSF88946. 1 hit.
TIGRFAMsTIGR02393. RpoD_Cterm. 1 hit.
TIGR02937. sigma70-ECF. 1 hit.
PROSITEPS00715. SIGMA70_1. 1 hit.
PS00716. SIGMA70_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSIGA_STAA8
AccessionPrimary (citable) accession number: P0A0J0
Secondary accession number(s): P26766, Q2FY12
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: February 19, 2014
This is version 69 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