P9WKD1 · PBPA_MYCTU
- ProteinPeptidoglycan D,D-transpeptidase PbpA
- GenepbpA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids491 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall (Probable). Required for the regulation of cell length. Plays critical roles for the survival of the pathogen inside the host. Required for both bacterial survival and formation of granuloma structures in a guinea pig infection model (PubMed:29530985).
Catalytic activity
Activity regulation
Inhibited by the antibiotics imipenem, penicillin G, and ceftriaxone.
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 222 | Acyl-ester intermediate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | penicillin binding | |
Molecular Function | peptidoglycan L,D-transpeptidase activity | |
Molecular Function | serine-type D-Ala-D-Ala carboxypeptidase activity | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidoglycan D,D-transpeptidase PbpA
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP9WKD1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-7 | Cytoplasmic | ||||
Sequence: MNASLRR | ||||||
Transmembrane | 8-28 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: ISVTVMALIVLLLLNATMTQV | ||||||
Topological domain | 29-491 | Periplasmic | ||||
Sequence: FTADGLRADPRNQRVLLDEYSRQRGQITAGGQLLAYSVATDGRFRFLRVYPNPEVYAPVTGFYSLRYSSTALERAEDPILNGSDRRLFGRRLADFFTGRDPRGGNVDTTINPRIQQAGWDAMQQGCYGPCKGAVVALEPSTGKILALVSSPSYDPNLLASHNPEVQAQAWQRLGDNPASPLTNRAISETYPPGSTFKVITTAAALAAGATETEQLTAAPTIPLPGSTAQLENYGGAPCGDEPTVSLREAFVKSCNTAFVQLGIRTGADALRSMARAFGLDSPPRPTPLQVAESTVGPIPDSAALGMTSIGQKDVALTPLANAEIAATIANGGITMRPYLVGSLKGPDLANISTTVGYQQRRAVSPQVAAKLTELMVGAEKVAQQKGAIPGVQIASKTGTAEHGTDPRHTPPHAWYIAFAPAQAPKVAVAVLVENGADRLSATGGALAAPIGRAVIEAALQGEP |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deletion of the gene does not impact in vitro growth, but it leads to aberrations in the cell length. Deletion mutant shows much higher sensitivity to oxacillin and clavulanic acid. Mutant shows compromised bacterial virulence in the host.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 281 | Can rescue the deletion mutant. | ||||
Sequence: S → A | ||||||
Mutagenesis | 424 | Cannot rescue the deletion mutant. | ||||
Sequence: K → G |
Miscellaneous
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000343832 | 1-491 | Peptidoglycan D,D-transpeptidase PbpA | |||
Sequence: MNASLRRISVTVMALIVLLLLNATMTQVFTADGLRADPRNQRVLLDEYSRQRGQITAGGQLLAYSVATDGRFRFLRVYPNPEVYAPVTGFYSLRYSSTALERAEDPILNGSDRRLFGRRLADFFTGRDPRGGNVDTTINPRIQQAGWDAMQQGCYGPCKGAVVALEPSTGKILALVSSPSYDPNLLASHNPEVQAQAWQRLGDNPASPLTNRAISETYPPGSTFKVITTAAALAAGATETEQLTAAPTIPLPGSTAQLENYGGAPCGDEPTVSLREAFVKSCNTAFVQLGIRTGADALRSMARAFGLDSPPRPTPLQVAESTVGPIPDSAALGMTSIGQKDVALTPLANAEIAATIANGGITMRPYLVGSLKGPDLANISTTVGYQQRRAVSPQVAAKLTELMVGAEKVAQQKGAIPGVQIASKTGTAEHGTDPRHTPPHAWYIAFAPAQAPKVAVAVLVENGADRLSATGGALAAPIGRAVIEAALQGEP | ||||||
Disulfide bond | 266↔282 | |||||
Sequence: CGDEPTVSLREAFVKSC |
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 160-484 | Transpeptidase | ||||
Sequence: GAVVALEPSTGKILALVSSPSYDPNLLASHNPEVQAQAWQRLGDNPASPLTNRAISETYPPGSTFKVITTAAALAAGATETEQLTAAPTIPLPGSTAQLENYGGAPCGDEPTVSLREAFVKSCNTAFVQLGIRTGADALRSMARAFGLDSPPRPTPLQVAESTVGPIPDSAALGMTSIGQKDVALTPLANAEIAATIANGGITMRPYLVGSLKGPDLANISTTVGYQQRRAVSPQVAAKLTELMVGAEKVAQQKGAIPGVQIASKTGTAEHGTDPRHTPPHAWYIAFAPAQAPKVAVAVLVENGADRLSATGGALAAPIGRAVIE |
Domain
The apo form can adopt multiple conformations (PubMed:22365933).
The beta5-alpha11 loop near the active site is a flexible region that can adopt a variety of conformations in the acylated state of PBPA and appears important for acylation (PubMed:22365933).
The beta5-alpha11 loop near the active site is a flexible region that can adopt a variety of conformations in the acylated state of PBPA and appears important for acylation (PubMed:22365933).
Sequence similarities
Belongs to the transpeptidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length491
- Mass (Da)51,576
- Last updated2014-04-16 v1
- Checksum888DBA26BE251581
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP42738.1 EMBL· GenBank· DDBJ | Genomic DNA |