P0C8P9 · THCL_STRSQ

  • Protein
    Thiocillin GE37468
  • Gene
    getA
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Has bacteriocidal activity against both aerobic and anaerobic Gram-positive bacteria. Inhibits growth of B.subtilis (MIC=0.047 ug/ml) and methicillin-resistant S.aureus (MRSA) (MIC=0.047 ug/ml). Has poor activity against Gram-negative bacteria, with the exception of B.fragilis. Inhibits bacterial protein biosynthesis by acting on elongation factor Tu (EF-Tu). Full antibiotic activity depends on the presence of the modified residue Ile-50.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functiontranslation repressor activity
Biological Processdefense response to Gram-negative bacterium
Biological Processdefense response to Gram-positive bacterium
Biological Processkilling of cells of another organism
Biological Processnegative regulation of translation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Thiocillin GE37468
  • Alternative names
    • Antibiotic GE37468

Gene names

    • Name
      getA

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 55365
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    P0C8P9
  • Secondary accessions
    • G1ECL0

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis50Two-fold decrease in antibiotic activity.

PTM/Processing

Features

Showing features for propeptide, cross-link, peptide, modified residue.

TypeIDPosition(s)Description
PropeptidePRO_00004149241-42Removed in mature form
Cross-link43↔445-methyloxazole-4-carboxylic acid (Ser-Thr)
Cross-link43↔52Pyridine-2,5-dicarboxylic acid (Ser-Cys) (with S-53)
Cross-link43↔53Pyridine-2,5-dicarboxylic acid (Ser-Ser) (with C-52)
PeptidePRO_000036317143-56Thiocillin GE37468
Cross-link45↔46Thiazole-4-carboxylic acid (Asn-Cys)
Cross-link47↔48Thiazoline-4-carboxylic acid (Phe-Cys)
Modified residue505-hydroxy-3-methylproline (Ile)
Cross-link50↔51Thiazole-4-carboxylic acid (Ile-Cys)
Cross-link51↔52Thiazole-4-carboxylic acid (Cys-Cys)
Cross-link53↔54Thiazole-4-carboxylic acid (Ser-Cys)
Modified residue552,3-didehydroalanine (Ser)
Modified residue562,3-didehydroalanine (Ser)
PropeptidePRO_000041492557Removed in mature form

Post-translational modification

Maturation of thiazole and oxazole containing antibiotics involves the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogenated to form thiazole or oxazole rings.
Maturation of pyridinyl containing antibiotics involves the cross-linking of a Ser and a Cys-Ser pair usually separated by 7 or 8 residues along the peptide chain. The Ser residues are dehydrated to didehydroalanines, then bonded between their beta carbons. The alpha carbonyl of the Cys condenses with alpha carbon of the first Ser to form a pyridinyl ring. The ring may be multiply dehydrogenated to form a pyridine ring with loss of the amino nitrogen of the first Ser.

Keywords

Family & Domains

Sequence similarities

Belongs to the thiocillin family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    57
  • Mass (Da)
    6,058
  • Last updated
    2012-01-25 v2
  • Checksum
    1B62126BDED6078B
MGNNEEYFIDVNDLSIDVFDVVEQGGAVTALTADHGMPEVGASTNCFCYICCSCSSN

Mass Spectrometry

Molecular mass is 1,309.48 Da. Determined by FAB.
Molecular mass is 1,308.247 Da. Determined by Electrospray.

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JN052143
EMBL· GenBank· DDBJ
AEM00614.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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