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Protein

Anti-sigma F factor

Gene

spoIIAB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Sporulation

Keywords - Ligandi

ATP-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

WithEntry#Exp.IntActNotes
O327285EBI-1033242,EBI-1033248
spoIIAAO327264EBI-1033242,EBI-1039369

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

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00637. Anti_sigma_F. 1 hit.
InterProiIPR010194. Anti-sigma_F.
IPR003594. HATPase_C.
[Graphical view]
PfamiPF13581. HATPase_c_2. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
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.

Cross-referencesi

Sequence databases

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

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...

Protein-protein interaction databases

IntActiO32727. 2 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO32727.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00637. Anti_sigma_F. 1 hit.
InterProiIPR010194. Anti-sigma_F.
IPR003594. HATPase_C.
[Graphical view]
PfamiPF13581. HATPase_c_2. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR01925. spIIAB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSP2AB_GEOSE
AccessioniPrimary (citable) accession number: O32727
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.