Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RNA polymerase sigma factor SigA

Gene

sigA

Organism
Thermus aquaticus
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.UniRule annotation2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi398 – 417H-T-H motifUniRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Sigma factor
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase sigma factor SigAUniRule annotation
Gene namesi
Name:sigAUniRule annotation
OrganismiThermus aquaticus
Taxonomic identifieri271 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004230111 – 438RNA polymerase sigma factor SigAAdd BLAST438

Proteomic databases

PRIDEiQ9EZJ8

Interactioni

Subunit structurei

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.UniRule annotation5 Publications

Protein-protein interaction databases

DIPiDIP-49014N
IntActiQ9EZJ8, 1 interactor

Structurei

Secondary structure

1438
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi94 – 103Combined sources10
Helixi111 – 135Combined sources25
Helixi139 – 148Combined sources10
Helixi151 – 153Combined sources3
Helixi168 – 179Combined sources12
Helixi183 – 204Combined sources22
Helixi207 – 214Combined sources8
Helixi215 – 217Combined sources3
Beta strandi220 – 222Combined sources3
Helixi224 – 241Combined sources18
Helixi244 – 246Combined sources3
Helixi250 – 269Combined sources20
Helixi277 – 297Combined sources21
Helixi303 – 310Combined sources8
Helixi316 – 326Combined sources11
Helixi344 – 346Combined sources3
Beta strandi351 – 353Combined sources3
Beta strandi370 – 372Combined sources3
Turni373 – 375Combined sources3
Helixi378 – 387Combined sources10
Turni388 – 392Combined sources5
Helixi398 – 405Combined sources8
Helixi409 – 425Combined sources17
Helixi434 – 437Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KU2X-ray2.90A/B92-332[»]
1KU3X-ray1.80A366-438[»]
1KU7X-ray2.40A/D366-438[»]
1L9UX-ray4.00H/Q92-438[»]
1L9ZX-ray6.50H1-438[»]
1RIOX-ray2.30H366-438[»]
3LESX-ray2.77A/B93-271[»]
3LEVX-ray2.50A93-271[»]
3N97X-ray3.25A/D366-438[»]
3UGOX-ray2.10A92-332[»]
3UGPX-ray2.70A92-332[»]
4KI2X-ray3.61A/B92-332[»]
4XLNX-ray4.00F/L92-438[»]
4XLPX-ray4.00F/L92-438[»]
4XLQX-ray4.60F/L92-438[»]
4XLRX-ray4.30F/L92-438[»]
4XLSX-ray4.01F/L92-438[»]
5TJGX-ray2.60F92-438[»]
ProteinModelPortaliQ9EZJ8
SMRiQ9EZJ8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9EZJ8

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 128Sigma-70 factor domain-1Add BLAST36
Regioni202 – 272Sigma-70 factor domain-2Add BLAST71
Regioni281 – 359Sigma-70 factor domain-3Add BLAST79
Regioni372 – 424Sigma-70 factor domain-4Add BLAST53

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi226 – 229Interaction with polymerase core subunit RpoC4

Domaini

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
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 (PubMed:11931761 and PubMed:22136875).
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 (PubMed:11931761).1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DG1 Bacteria
COG0568 LUCA

Family and domain databases

Gene3Di1.10.10.10, 2 hits
HAMAPiMF_00963 Sigma70_RpoD_SigA, 1 hit
InterProiView protein in InterPro
IPR014284 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
IPR013325 RNA_pol_sigma_r2
IPR013324 RNA_pol_sigma_r3/r4-like
IPR012760 RNA_pol_sigma_RpoD_C
IPR028630 Sigma70_RpoD
IPR036388 WH-like_DNA-bd_sf
PfamiView protein in Pfam
PF00140 Sigma70_r1_2, 1 hit
PF04542 Sigma70_r2, 1 hit
PF04539 Sigma70_r3, 1 hit
PF04545 Sigma70_r4, 1 hit
PRINTSiPR00046 SIGMA70FCT
SUPFAMiSSF88659 SSF88659, 2 hits
SSF88946 SSF88946, 1 hit
TIGRFAMsiTIGR02393 RpoD_Cterm, 1 hit
TIGR02937 sigma70-ECF, 1 hit
PROSITEiView protein in PROSITE
PS00716 SIGMA70_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9EZJ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKSKSKKKA AKAQEVEVKE PVKEPEPLPE LEAAEDLQDL PEPDPELLAS
60 70 80 90 100
EPELEDLADP LDLEGPLEAD LLPEEGLLEE EEEELSLPKV STSDPVRQYL
110 120 130 140 150
HEIGQVPLLT LEEEIDLARK VEEGMEAIKK LSEATGLDQE LIREVVRAKI
160 170 180 190 200
LGTARIQKIP GLKEKPDPKT VEEVDGKLKS LPKELKRYLH IAREGEAARQ
210 220 230 240 250
HLIEANLRLV VSIAKKYTGR GLSFLDLIQE GNQGLIRAVE KFEYKRRFKF
260 270 280 290 300
STYATWWIRQ AINRAIADQA RTIRIPVHMV ETINKLSRTA RQLQQELGRE
310 320 330 340 350
PSYEEIAEAM GPGWDAKRVE ETLKIAQEPV SLETPIGDEK DSFYGDFIPD
360 370 380 390 400
ENLPSPVEAA AQSLLSEELE KALSKLSERE AMVLKLRKGL IDGREHTLEE
410 420 430
VGAYFGVTRE RIRQIENKAL RKLKYHESRT RKLRDFLE
Length:438
Mass (Da):49,847
Last modified:March 1, 2001 - v1
Checksum:i5D8ACF5713DE55AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291720 Genomic DNA Translation: AAG36964.1

Similar proteinsi

Entry informationi

Entry nameiSIGA_THEAQ
AccessioniPrimary (citable) accession number: Q9EZJ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health