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Protein

Anti-sigma F factor

Gene

spoIIAB

Organism
Bacillus subtilis (strain 168)
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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

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

Enzyme and pathway databases

BioCyciBSUB:BSU23460-MONOMER.

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
Ordered Locus Names:BSU23460
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU23460. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146Anti-sigma F factorPRO_0000203561Add
BLAST

Proteomic databases

PaxDbiP10728.

Expressioni

Developmental stagei

Interaction with SpoIIAB inhibits sigma F activity throughout the cell before the formation of the asymmetric septum; after septation the interaction is confined to the mother cell, and sigma F activity is released in the prespore.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ybdMO314352EBI-9344705,EBI-5255200

Protein-protein interaction databases

IntActiP10728. 5 interactions.
STRINGi224308.Bsubs1_010100012876.

Structurei

3D structure databases

ProteinModelPortaliP10728.
SMRiP10728. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the anti-sigma-factor family.Curated

Phylogenomic databases

eggNOGiCOG2172.
HOGENOMiHOG000269931.
InParanoidiP10728.
KOiK06379.
OMAiHAYEDKI.
OrthoDBiEOG6S7XW5.
PhylomeDBiP10728.

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.

P10728-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNEMHLEFS ALSQNESFAR VTVASFIAQL DPTMDELTEI KTVVSEAVTN
60 70 80 90 100
AIIHGYEENC EGKVYISVTL EDHVVYMTIR DEGLGITDLE EARQPLFTTK
110 120 130 140
PELERSGMGF TIMENFMDDV SIDSSPEMGT TIRLTKHLSK SKALCN
Length:146
Mass (Da):16,356
Last modified:February 1, 1991 - v1
Checksum:i141A28D41EDEC997
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17643 Genomic DNA. Translation: AAA22790.1.
D84432 Genomic DNA. Translation: BAA12654.1.
AL009126 Genomic DNA. Translation: CAB14278.1.
PIRiB55646.
RefSeqiNP_390227.1. NC_000964.3.
WP_003230452.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14278; CAB14278; BSU23460.
GeneIDi938930.
KEGGibsu:BSU23460.
PATRICi18976511. VBIBacSub10457_2446.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17643 Genomic DNA. Translation: AAA22790.1.
D84432 Genomic DNA. Translation: BAA12654.1.
AL009126 Genomic DNA. Translation: CAB14278.1.
PIRiB55646.
RefSeqiNP_390227.1. NC_000964.3.
WP_003230452.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP10728.
SMRiP10728. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP10728. 5 interactions.
STRINGi224308.Bsubs1_010100012876.

Proteomic databases

PaxDbiP10728.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14278; CAB14278; BSU23460.
GeneIDi938930.
KEGGibsu:BSU23460.
PATRICi18976511. VBIBacSub10457_2446.

Organism-specific databases

GenoListiBSU23460. [Micado]

Phylogenomic databases

eggNOGiCOG2172.
HOGENOMiHOG000269931.
InParanoidiP10728.
KOiK06379.
OMAiHAYEDKI.
OrthoDBiEOG6S7XW5.
PhylomeDBiP10728.

Enzyme and pathway databases

BioCyciBSUB:BSU23460-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of sporulation locus spoIIA in Bacillus subtilis."
    Fort P., Piggot P.J.
    J. Gen. Microbiol. 130:2147-2153(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
    Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
    Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH642.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "SpoIIAB is an anti-sigma factor that binds to and inhibits transcription by regulatory protein sigma F from Bacillus subtilis."
    Duncan L., Losick R.
    Proc. Natl. Acad. Sci. U.S.A. 90:2325-2329(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Sigma F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-sigma factor that is also a protein kinase."
    Min K.-T., Hilditch C.M., Diederich B., Errington J., Yudkin M.D.
    Cell 74:735-742(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEIN SEQUENCE OF 1-14.
    Strain: CU267.

Entry informationi

Entry nameiSP2AB_BACSU
AccessioniPrimary (citable) accession number: P10728
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 24, 2015
This is version 114 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.