D0L235 · D0L235_HALNC
- ProteinPenicillin-binding protein 1A
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids790 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
GO annotations
Aspect | Term | |
---|---|---|
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 | peptidoglycan biosynthetic process | |
Biological Process | proteolysis | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePenicillin-binding protein 1A
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Chromatiales > Halothiobacillaceae > Halothiobacillus
Accessions
- Primary accessionD0L235
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Single-pass type II membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 7-29 | Helical | ||||
Sequence: VVYVFGFLLIFSVGGVGILYQIY |
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 55-229 | Glycosyl transferase family 51 | ||||
Sequence: GGLIAEFGEKRRFPVTYAELPKVVVDAFTSAEDGGFFEHGGVDVQSLFRAAYELVKTGHKGQGGSTITMQVARNFFLGRQKTYSRKLMEILLAIKIEHTLSKEQILTLYLNKIFLGNRTYGVKAAAQVYFGKSLDKLTVAEAAMLASLPKAPSSVNPVSNPDKALARRAYVLGRM | ||||||
Domain | 317-423 | Penicillin-binding protein OB-like | ||||
Sequence: YRGAEDHWGSLLSDPKALLDKLQDTPVVGGLIPAVVLSVDPKTAVVLMPDGSKNSLGMDAVSWACRYESTDHCGPKPKLMGDVLKAGDLIRLQAEADQHWMLAEIPA | ||||||
Domain | 427-683 | Penicillin-binding protein transpeptidase | ||||
Sequence: GFVALDPETGAIRALVGGFDFAHDSKFNHVTQAERQPGSGFKPFLYSAALDHGFTLATMINDSPVVVKNGVKEGVDWRPQNYEKHFGGPMRLRMALVHSVNLVSIRLIEALGPENVLKYASRFGLPTQNWSPTPSMALGSYTLTPLELVGGFSAFVNGGFRITPYVITEVDNGDNAVLYSHPSVNLCDTCPMDSPDPSVAPRIITPQNAFLMRSALRDVVRMGTGVRAYRALKRDDIGGKTGTTNEQRDAWFTGFGP |
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
- Length790
- Mass (Da)86,138
- Last updated2009-12-15 v1
- Checksum55C852FA433108EE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001801 EMBL· GenBank· DDBJ | ACX96758.1 EMBL· GenBank· DDBJ | Genomic DNA |