A0A4U0YQ29 · A0A4U0YQ29_9GAMM
- ProteinPenicillin-binding protein 1B
- GenemrcB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids821 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Catalytic activity
- [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H+
[GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate RHEA-COMP:9602 + CHEBI:60033 = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate RHEA-COMP:9603 + CHEBI:58405 + CHEBI:15378
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 237 | Proton donor; for transglycosylase activity | |||
Active site | 515 | Acyl-ester intermediate; for transpeptidase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | peptidoglycan-based cell wall | |
Molecular Function | penicillin binding | |
Molecular Function | peptidoglycan glycosyltransferase activity | |
Molecular Function | serine-type D-Ala-D-Ala carboxypeptidase activity | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | proteolysis | |
Biological Process | regulation of cell shape | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePenicillin-binding protein 1B
- Short namesPBP-1b ; PBP1b
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Chromatiales > Thioalkalibacteraceae > Guyparkeria
Accessions
- Primary accessionA0A4U0YQ29
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 66-88 | Helical | |||
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | |||
Region | 1-56 | Disordered | |||
Compositional bias | 34-49 | Polar residues | |||
Domain | 115-198 | Bifunctional transglycosylase second | |||
Domain | 211-384 | Glycosyl transferase family 51 | |||
Domain | 479-717 | Penicillin-binding protein transpeptidase | |||
Sequence similarities
In the C-terminal section; belongs to the transpeptidase family.
In the N-terminal section; belongs to the glycosyltransferase 51 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length821
- Mass (Da)90,454
- Last updated2019-07-31 v1
- Checksum80F500571084AE54
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | |||
Compositional bias | 34-49 | Polar residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SWAW01000003 EMBL· GenBank· DDBJ | TKA91103.1 EMBL· GenBank· DDBJ | Genomic DNA |