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P02966 (DESS_MYXXA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 11, 2011. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Development-specific protein S
Alternative name(s):
Spore coat protein S
Gene names
Name:tps
OrganismMyxococcus xanthus
Taxonomic identifier34 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeMyxococcus

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.

Cofactor

Binds 2 calcium ions per subunit.

Domain

Has a two-domain beta-structure, folded into four very similar Greek key motifs.

Sequence similarities

Belongs to the beta/gamma-crystallin family.

Contains 4 beta/gamma crystallin 'Greek key' domains.

Ontologies

Keywords
   Biological processSporulation
   DomainRepeat
   LigandCalcium
   Technical term3D-structure
Gene Ontology (GO)
   Biological processsporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 173173Development-specific protein S
PRO_0000057606

Regions

Domain2 – 4645Beta/gamma crystallin 'Greek key' 1
Domain48 – 8639Beta/gamma crystallin 'Greek key' 2
Domain91 – 13545Beta/gamma crystallin 'Greek key' 3
Domain136 – 17338Beta/gamma crystallin 'Greek key' 4
Calcium binding32 – 4615 Probable
Calcium binding121 – 13515 Probable
Region87 – 904Connecting peptide

Experimental info

Mutagenesis401S → R: Suppresses completely calcium-binding.
Mutagenesis1291S → R: Lower calcium affinity.

Secondary structure

................................... 173
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02966 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: C504A6409752C454

FASTA17318,793
        10         20         30         40         50         60 
MANITVFYNE DFQGKQVDLP PGNYTRAQLA ALGIENNTIS SVKVPPGVKA ILYQNDGFAG 

        70         80         90        100        110        120 
DQIEVVANAE ELGPLNNNVS SIRVISVPVQ PRARFFYKEQ FDGKEVDLPP GQYTQAELER 

       130        140        150        160        170 
YGIDNNTISS VKPQGLAVVL FKNDNFSGDT LPVNSDAPTL GAMNNNTSSI RIS 

« Hide

References

[1]"Structural similarities between the development-specific protein S from a Gram-negative bacterium, Myxococcus xanthus, and calmodulin."
Inouye S., Franceschini T., Inouye M.
Proc. Natl. Acad. Sci. U.S.A. 80:6829-6833(1983) [PubMed: 6316328] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of calcium-binding sites in development-specific protein S of Myxococcus xanthus using site-specific mutagenesis."
Teintze M., Inouye M., Inouye S.
J. Biol. Chem. 263:1199-1203(1988) [PubMed: 3121626] [Abstract]
Cited for: CALCIUM-BINDING SITES, MUTAGENESIS.
[3]"Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens beta gamma-crystallins."
Wistow G., Summers L., Blundell T.
Nature 315:771-773(1985) [PubMed: 3925350] [Abstract]
Cited for: SIMILARITY TO BETA/GAMMA-CRYSTALLIN FAMILY.
[4]"Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens."
Bagby S., Harvey T.S., Eagle S.G., Inouye S., Ikura M.
Proc. Natl. Acad. Sci. U.S.A. 91:4308-4312(1994) [PubMed: 8183906] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"NMR-derived three-dimensional solution structure of protein S complexed with calcium."
Bagby S., Harvey T.S., Eagle S.G., Inouye S., Ikura M.
Structure 2:107-122(1994) [PubMed: 8081742] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01745 Genomic DNA. Translation: AAA25407.1.
PIRDZYZSX. A03490.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NPSX-ray1.80A2-89[»]
1PRRNMR-A1-173[»]
1PRSNMR-A1-173[»]
ProteinModelPortalP02966.
SMRP02966. Positions 1-173.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
Gene3DG3DSA:2.60.20.10. Crystallin. 2 hits.
PfamPF00030. Crystall. 2 hits.
[Graphical view]
SMARTSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMSSF49695. G_crystallin_SF. 2 hits.
PROSITEPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDESS_MYXXA
AccessionPrimary (citable) accession number: P02966
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 11, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families