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P10727

- SP2AA_BACSU

UniProt

P10727 - SP2AA_BACSU

Protein

Anti-sigma F factor antagonist

Gene

spoIIAA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition.1 Publication

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: InterPro
    2. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Biological processi

    Sporulation

    Enzyme and pathway databases

    BioCyciBSUB:BSU23470-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anti-sigma F factor antagonist
    Alternative name(s):
    Stage II sporulation protein AA
    Gene namesi
    Name:spoIIAA
    Ordered Locus Names:BSU23470
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU23470. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 117116Anti-sigma F factor antagonistPRO_0000194204Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by SpoIIAB on a serine residue.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP10727.

    PTM databases

    PhosSiteiP010322.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU23470.

    Structurei

    Secondary structure

    1
    117
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Beta strandi13 – 164
    Helixi26 – 3813
    Beta strandi45 – 495
    Helixi60 – 7415
    Turni85 – 884
    Helixi89 – 946
    Helixi97 – 993
    Helixi106 – 1083
    Helixi110 – 1123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AUZNMR-A2-117[»]
    1BUZNMR-A2-117[»]
    ProteinModelPortaliP10727.
    SMRiP10727. Positions 2-117.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10727.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 113111STASPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 STAS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1366.
    HOGENOMiHOG000270156.
    KOiK06378.
    OMAiHLEVKRD.
    OrthoDBiEOG6J48NK.
    PhylomeDBiP10727.

    Family and domain databases

    Gene3Di3.30.750.24. 1 hit.
    InterProiIPR003658. Anti-sigma_ant.
    IPR014237. Anti-sigma_F_ant.
    IPR002645. STAS_dom.
    [Graphical view]
    PfamiPF01740. STAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52091. SSF52091. 1 hit.
    TIGRFAMsiTIGR00377. ant_ant_sig. 1 hit.
    TIGR02886. spore_II_AA. 1 hit.
    PROSITEiPS50801. STAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P10727-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLGIDMNVK ESVLCIRLTG ELDHHTAETL KQKVTQSLEK DDIRHIVLNL    50
    EDLSFMDSSG LGVILGRYKQ IKQIGGEMVV CAISPAVKRL FDMSGLFKII 100
    RFEQSEQQAL LTLGVAS 117
    Length:117
    Mass (Da):12,990
    Last modified:January 23, 2007 - v3
    Checksum:i2333E74207568AC2
    GO

    Sequence cautioni

    The sequence AAA22789.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17643 Genomic DNA. Translation: AAA22789.1. Different initiation.
    D84432 Genomic DNA. Translation: BAA12653.1.
    AL009126 Genomic DNA. Translation: CAB14279.1.
    PIRiA55646.
    RefSeqiNP_390228.1. NC_000964.3.
    WP_004398633.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14279; CAB14279; BSU23470.
    GeneIDi938730.
    KEGGibsu:BSU23470.
    PATRICi18976513. VBIBacSub10457_2447.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17643 Genomic DNA. Translation: AAA22789.1 . Different initiation.
    D84432 Genomic DNA. Translation: BAA12653.1 .
    AL009126 Genomic DNA. Translation: CAB14279.1 .
    PIRi A55646.
    RefSeqi NP_390228.1. NC_000964.3.
    WP_004398633.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AUZ NMR - A 2-117 [» ]
    1BUZ NMR - A 2-117 [» ]
    ProteinModelPortali P10727.
    SMRi P10727. Positions 2-117.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU23470.

    PTM databases

    PhosSitei P010322.

    Proteomic databases

    PaxDbi P10727.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14279 ; CAB14279 ; BSU23470 .
    GeneIDi 938730.
    KEGGi bsu:BSU23470.
    PATRICi 18976513. VBIBacSub10457_2447.

    Organism-specific databases

    GenoListi BSU23470. [Micado ]

    Phylogenomic databases

    eggNOGi COG1366.
    HOGENOMi HOG000270156.
    KOi K06378.
    OMAi HLEVKRD.
    OrthoDBi EOG6J48NK.
    PhylomeDBi P10727.

    Enzyme and pathway databases

    BioCyci BSUB:BSU23470-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P10727.

    Family and domain databases

    Gene3Di 3.30.750.24. 1 hit.
    InterProi IPR003658. Anti-sigma_ant.
    IPR014237. Anti-sigma_F_ant.
    IPR002645. STAS_dom.
    [Graphical view ]
    Pfami PF01740. STAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52091. SSF52091. 1 hit.
    TIGRFAMsi TIGR00377. ant_ant_sig. 1 hit.
    TIGR02886. spore_II_AA. 1 hit.
    PROSITEi PS50801. STAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
      Strain: CU267.
    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. "Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase sigma factor and for a putative DD-carboxypeptidase."
      Wu J.-J., Schuch R., Piggot P.J.
      J. Bacteriol. 174:4885-4892(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-4.
    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 2-14.
    6. "Site of phosphorylation of SpoIIAA, the anti-anti-sigma factor for sporulation-specific sigma F of Bacillus subtilis."
      Najafi S.M.A., Willis A.C., Yudkin M.D.
      J. Bacteriol. 177:2912-2913(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-58, PROTEIN SEQUENCE OF 52-67.
    7. "Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigmaF of Bacillus subtilis."
      Kovacs H., Comfort D., Lord M., Campbell I.D., Yudkin M.D.
      Proc. Natl. Acad. Sci. U.S.A. 95:5067-5071(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiSP2AA_BACSU
    AccessioniPrimary (citable) accession number: P10727
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3