SubmitCancel

Skip Header

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

O32727

- SP2AB_GEOSE

UniProt

O32727 - SP2AB_GEOSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 By similarity.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. protein serine/threonine kinase activity Source: UniProtKB-KW
  4. 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 factor (EC:2.7.11.1)
Alternative name(s):
Stage II sporulation protein AB
Gene namesi
Name:spoIIAB
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146Anti-sigma F factorUniRule annotation
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiO32727.

Family & Domainsi

Sequence similaritiesi

Belongs to the anti-sigma-factor family.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00637. Anti_sigma_F.
InterProiIPR010194. Anti-sigma_F.
IPR003594. HATPase_ATP-bd.
[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

MRNEMHLQFS ARSENESFAR VTVAAFVAQL DPTTDELTEI KTVVSEAVTN    50
AIIHGYNNDP NGIVSISVII EDGVVHLTVR DEGVGIPDIE EARQPLFTTK 100
PELERSGMGF TIMENFMDEV IVESEVNKGT TVYLKKAYCE KQTLCN 146
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_ATP-bd.
[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: June 11, 2014
This is version 82 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

Similar proteinsi