A0AA37JS94 · A0AA37JS94_9FIRM
- ProteinPenicillin-binding protein 1A
- GenemrcA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids895 (go to sequence)
- Protein existencePredicted
- 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
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | penicillin binding | |
Biological Process | proteolysis | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePenicillin-binding protein 1A
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Hungatella
Accessions
- Primary accessionA0AA37JS94
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type II membrane protein
Membrane ; Single-pass type II membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 26-53 | Helical | ||||
Sequence: VFLAFLKSLFVLCLFCLVVAGSIGFGMV |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 85-264 | Glycosyl transferase family 51 | ||||
Sequence: TETLVTAGSNREEASYDELPGNLINAFVAYEDARFWEHNGIDLRSIMRAVKGVLTGDSSAGGGSTITQQLIKNSVFGGGMEKSFGERLERKMQEWYLAVKLDSAMSKEQIITNYLNTINLGKNSLGVKVAARRYFNKEVSDLTLSECAVLAGITQNPSKFNPVTGQKANSDKQKVILQYM | ||||||
Domain | 442-728 | Penicillin-binding protein transpeptidase | ||||
Sequence: SFVIMDQKTGQVKAIAGGRGEKTASLTLNRASNTLRQPGSTFKVLTAFAPAMDTCGATLGTVYYDSVYTVGKKTFSNWYSSGYQGYSSIRDGIIYSMNIVAVRCLMETVTPQLGVEYAKNFGITSLTDTDYNAALALGGITDGVSNLEMTAAYATIANGGVYTKPVFFTKIIDHNGKVLIDNTPETHRVLKDSTAFLLTDAMADSMESSRKFARPGAGPSSTSSSANIPGMSNAGKSGTTTSNNDIWFVGYTPYYTAGIWGGCDNNQKLTKKNGGTSFHKAIWKKIM | ||||||
Region | 649-679 | Disordered | ||||
Sequence: SSRKFARPGAGPSSTSSSANIPGMSNAGKSG | ||||||
Compositional bias | 656-679 | Polar residues | ||||
Sequence: PGAGPSSTSSSANIPGMSNAGKSG | ||||||
Region | 848-895 | Disordered | ||||
Sequence: IPPSDDTGMPETVAPGTLPYGPGYVSPNTQTSPAPPAGSPVQMSPGGQ | ||||||
Compositional bias | 870-884 | Polar residues | ||||
Sequence: GYVSPNTQTSPAPPA |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length895
- Mass (Da)97,007
- Last updated2024-01-24 v1
- Checksum1E84DA5F240C36AF
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 656-679 | Polar residues | ||||
Sequence: PGAGPSSTSSSANIPGMSNAGKSG | ||||||
Compositional bias | 870-884 | Polar residues | ||||
Sequence: GYVSPNTQTSPAPPA |