A0A366YQZ3 · A0A366YQZ3_ECOLX
- ProteinPenicillin-binding protein 1B
- GenemrcB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids842 (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 | 231 | Proton donor; for transglycosylase activity | |||
Active site | 508 | Acyl-ester intermediate; for transpeptidase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | outer membrane-bounded periplasmic space | |
Cellular Component | peptidoglycan-based cell wall | |
Cellular Component | plasma membrane | |
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A366YQZ3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 63-84 | Helical | |||
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-10 | Basic and acidic residues | |||
Region | 1-58 | Disordered | |||
Domain | 1-77 | Transglycosylase PBP1b N-terminal transmembrane | |||
Compositional bias | 11-25 | Basic residues | |||
Compositional bias | 30-44 | Acidic residues | |||
Compositional bias | 48-58 | Basic residues | |||
Domain | 111-195 | Bifunctional transglycosylase second | |||
Domain | 207-377 | Glycosyl transferase family 51 | |||
Domain | 471-712 | Penicillin-binding protein transpeptidase | |||
Region | 791-842 | Disordered | |||
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
Family and domain databases
Sequence
- Sequence statusComplete
- Length842
- Mass (Da)94,088
- Last updated2018-11-07 v1
- MD5 Checksum24CFFD9D48806A970D01AC92B8D60F1C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-10 | Basic and acidic residues | |||
Compositional bias | 11-25 | Basic residues | |||
Compositional bias | 30-44 | Acidic residues | |||
Compositional bias | 48-58 | Basic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ABKSHZ030000009 EMBL· GenBank· DDBJ | EMM9723109.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAAGYP010000025 EMBL· GenBank· DDBJ | NEN71968.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
SERV01000009 EMBL· GenBank· DDBJ | RYL81494.1 EMBL· GenBank· DDBJ | Genomic DNA |