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Protein

Anti-sigma F factor

Gene

spoIIAB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.UniRule annotation

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processSporulation
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Anti-sigma F factorUniRule annotation (EC:2.7.11.1UniRule annotation)
Alternative name(s):
Stage II sporulation protein ABUniRule annotation
Gene namesi
Name:spoIIABUniRule annotation
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002035601 – 146Anti-sigma F factorAdd BLAST146

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

IntActiO32727, 2 interactors

Structurei

Secondary structure

1146
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi15 – 27Combined sources13
Helixi28 – 30Combined sources3
Helixi34 – 53Combined sources20
Beta strandi56 – 58Combined sources3
Beta strandi62 – 71Combined sources10
Beta strandi74 – 81Combined sources8
Helixi89 – 92Combined sources4
Turni101 – 104Combined sources4
Helixi109 – 116Combined sources8
Beta strandi117 – 125Combined sources9
Turni126 – 128Combined sources3
Beta strandi129 – 136Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L0OX-ray2.90A/B1-142[»]
1TH8X-ray2.40A1-136[»]
1THNX-ray2.50A/C1-136[»]
1TIDX-ray2.50A/C1-136[»]
1TILX-ray2.70A/C/E1-146[»]
ProteinModelPortaliO32727
SMRiO32727
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32727

Family & Domainsi

Sequence similaritiesi

Belongs to the anti-sigma-factor family.UniRule annotation

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
Gene3Di3.30.565.10, 1 hit
HAMAPiMF_00637 Anti_sigma_F, 1 hit
InterProiView protein in InterPro
IPR010194 Anti-sigma_F
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
PANTHERiPTHR35526:SF2 PTHR35526:SF2, 1 hit
PfamiView protein in Pfam
PF13581 HATPase_c_2, 1 hit
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SUPFAMiSSF55874 SSF55874, 1 hit
TIGRFAMsiTIGR01925 spIIAB, 1 hit

Sequencei

Sequence statusi: Complete.

O32727-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNEMHLQFS ARSENESFAR VTVAAFVAQL DPTTDELTEI KTVVSEAVTN
60 70 80 90 100
AIIHGYNNDP NGIVSISVII EDGVVHLTVR DEGVGIPDIE EARQPLFTTK
110 120 130 140
PELERSGMGF TIMENFMDEV IVESEVNKGT TVYLKKAYCE KQTLCN
Length:146
Mass (Da):16,239
Last modified:January 1, 1998 - v1
Checksum:iB3F1BD38A9044416
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47360 Genomic DNA Translation: AAB81193.1

Similar proteinsi

Entry informationi

Entry nameiSP2AB_GEOSE
AccessioniPrimary (citable) accession number: O32727
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 23, 2018
This is version 94 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

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