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O32727

- SP2AB_GEOSE

UniProt

O32727 - SP2AB_GEOSE

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Protein

Anti-sigma F factor

Gene

spoIIAB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB-KW
  3. sigma factor antagonist activity Source: InterPro

GO - Biological processi

  1. negative regulation of transcription, DNA-templated Source: InterPro
  2. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146Anti-sigma F factorPRO_0000203560Add
BLAST

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

IntActiO32727. 2 interactions.

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119
Helixi15 – 2713
Helixi28 – 303
Helixi34 – 5320
Beta strandi56 – 583
Beta strandi62 – 7110
Beta strandi74 – 818
Helixi89 – 924
Turni101 – 1044
Helixi109 – 1168
Beta strandi117 – 1259
Turni126 – 1283
Beta strandi129 – 1368

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-136.
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.
InterProiIPR010194. Anti-sigma_F.
IPR003594. HATPase_C.
[Graphical view]
PfamiPF02518. HATPase_c. 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:
EMBL
GenBank
DDBJ
Links Updated
L47360 Genomic DNA. Translation: AAB81193.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L47360 Genomic DNA. Translation: AAB81193.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1L0O X-ray 2.90 A/B 1-142 [» ]
1TH8 X-ray 2.40 A 1-136 [» ]
1THN X-ray 2.50 A/C 1-136 [» ]
1TID X-ray 2.50 A/C 1-136 [» ]
1TIL X-ray 2.70 A/C/E 1-146 [» ]
ProteinModelPortali O32727.
SMRi O32727. Positions 1-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O32727. 2 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O32727.

Family and domain databases

Gene3Di 3.30.565.10. 1 hit.
HAMAPi MF_00637. Anti_sigma_F.
InterProi IPR010194. Anti-sigma_F.
IPR003594. HATPase_C.
[Graphical view ]
Pfami PF02518. HATPase_c. 1 hit.
[Graphical view ]
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF55874. SSF55874. 1 hit.
TIGRFAMsi TIGR01925. spIIAB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Sequencing and phylogenetic analysis of the spoIIA operon from diverse Bacillus and Paenibacillus species."
    Park S.G., Yudkin M.D.
    Gene 194:25-33(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 12980 / DSM 22 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / VKM B-510.

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: October 29, 2014
This is version 84 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

External Data

Dasty 3