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Protein

Sporulation inhibitor sda

Gene

sda

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

Functioni

Mediates a developmental checkpoint inhibiting initiation of sporulation (by preventing phosphorylation of spo0A) in response to defects in the replication initiation machinery. Inhibits autophosphorylation of the histidine protein kinase KinA, forming a molecular barricade that prevents productive interaction between the ATP-binding site in the catalytic domain and the phosphorylatable His in the phosphotransfer domain of KinA. Probably also inhibits the activity of KinB, but has relatively little effect on KinC. Has at least one target in vivo in addition to KinA as sda does not require KinA to inhibit sporulation.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251KinACurated
Binding sitei27 – 271KinACurated
Binding sitei31 – 311KinACurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protein kinase inhibitor

Keywords - Biological processi

Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU25690-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sporulation inhibitor sda
Alternative name(s):
Histidine kinase KinA inhibitor
Gene namesi
Name:sda
Ordered Locus Names:BSU25690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251M → A or I: Partial loss of ability to inhibit KinA autophosphorylation. 1 Publication
Mutagenesisi27 – 271L → A or E: Complete loss of ability to inhibit KinA autophosphorylation. 1 Publication
Mutagenesisi31 – 311F → H: Complete loss of ability to inhibit KinA autophosphorylation. 1 Publication
Mutagenesisi34 – 341L → A: Partial loss of ability to inhibit KinA autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5252Sporulation inhibitor sdaPRO_0000022288Add
BLAST

Proteomic databases

PaxDbiQ7WY62.

Interactioni

Subunit structurei

Forms a stable heterotetramer with KinA (comprising two molecules of each protein), by binding to the KinA dimerization/phosphotransfer domain.

Binary interactionsi

WithEntry#Exp.IntActNotes
kinAP164976EBI-6405714,EBI-6405707

Protein-protein interaction databases

IntActiQ7WY62. 1 interaction.

Structurei

Secondary structure

1
52
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 2413Combined sources
Helixi29 – 4315Combined sources
Turni45 – 495Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PV0NMR-A7-52[»]
3FYRX-ray1.97A/B/C7-52[»]
ProteinModelPortaliQ7WY62.
SMRiQ7WY62. Positions 9-47.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7WY62.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000262075.
KOiK06371.
OMAiDLLMETY.
OrthoDBiEOG6TTVVD.

Family and domain databases

InterProiIPR015064. Sda.
[Graphical view]
PfamiPF08970. Sda. 1 hit.
[Graphical view]
SUPFAMiSSF100985. SSF100985. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q7WY62-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNWVPSMRKL SDELLIESYF KATEMNLNRD FIELIENEIK RRSLGHIISV

SS
Length:52
Mass (Da):6,155
Last modified:October 1, 2003 - v1
Checksum:iBCBDECF0E0203CAE
GO
Isoform 2 (identifier: Q7WY62-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.

Note: No experimental confirmation available. Seems to be the major isoform.
Show »
Length:46
Mass (Da):5,440
Checksum:i1E9AE14098D07C69
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66Missing in isoform 2. CuratedVSP_018790

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAE01463.1.
RefSeqiWP_010886571.1. NC_000964.3. [Q7WY62-1]
YP_054588.1. NC_000964.3. [Q7WY62-1]

Genome annotation databases

EnsemblBacteriaiCAE01463; CAE01463; BSU25690.
GeneIDi2914223.
KEGGibsu:BSU25690.
PATRICi18976980. VBIBacSub10457_2679.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAE01463.1.
RefSeqiWP_010886571.1. NC_000964.3. [Q7WY62-1]
YP_054588.1. NC_000964.3. [Q7WY62-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PV0NMR-A7-52[»]
3FYRX-ray1.97A/B/C7-52[»]
ProteinModelPortaliQ7WY62.
SMRiQ7WY62. Positions 9-47.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7WY62. 1 interaction.

Proteomic databases

PaxDbiQ7WY62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE01463; CAE01463; BSU25690.
GeneIDi2914223.
KEGGibsu:BSU25690.
PATRICi18976980. VBIBacSub10457_2679.

Phylogenomic databases

HOGENOMiHOG000262075.
KOiK06371.
OMAiDLLMETY.
OrthoDBiEOG6TTVVD.

Enzyme and pathway databases

BioCyciBSUB:BSU25690-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ7WY62.

Family and domain databases

InterProiIPR015064. Sda.
[Graphical view]
PfamiPF08970. Sda. 1 hit.
[Graphical view]
SUPFAMiSSF100985. SSF100985. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "Replication initiation proteins regulate a developmental checkpoint in Bacillus subtilis."
    Burkholder W.F., Kurtser I., Grossman A.D.
    Cell 104:269-279(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, FUNCTION.
    Strain: 168 / JH642.
  3. "Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis."
    Rowland S.L., Burkholder W.F., Cunningham K.A., Maciejewski M.W., Grossman A.D., King G.F.
    Mol. Cell 13:689-701(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 7-52, FUNCTION, INTERACTION WITH KINA, MUTAGENESIS OF MET-25; LEU-27; PHE-31 AND LEU-34.

Entry informationi

Entry nameiSDA_BACSU
AccessioniPrimary (citable) accession number: Q7WY62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: October 1, 2003
Last modified: July 6, 2016
This is version 81 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, Complete proteome, 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

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.