A0A2S7IV89 · A0A2S7IV89_9HYPH
- ProteinPenicillin-binding protein 1A
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids819 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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 | 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
Names & Taxonomy
Protein names
- Recommended namePenicillin-binding protein 1A
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella
Accessions
- Primary accessionA0A2S7IV89
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner 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 | 6-27 | Helical | ||||
Sequence: GYFFGIGTVLMLLVAGGVALYV |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 56-233 | Glycosyl transferase family 51 | ||||
Sequence: GSLMAEFARERRLYIPIQAVPNRVKAAFVSAEDKTFYEHHGLDFAGLARAMITNVKNMGSGRRPVGASTITQQVAKNFLLTSKQTYDRKIKEAILAMRIEQAYSKDRILELYLNEIFFGLGSYGIASAALTYFDKSVGELSIAESAYLAALPKGPNNYHPFRQPERAIERRNWVIDRM | ||||||
Domain | 322-438 | Penicillin-binding protein OB-like | ||||
Sequence: WRGPMKNVELGNDWGTAFGDMQSYGDIPEWQLAIVLNVSAAGADIGLQPPLEASGSRSKERKRAFIAADDMKWAMRVVNIGGKRTSAKSPEGVLKAGDIIYVSKQGESRFRLQQPPK | ||||||
Domain | 441-734 | Penicillin-binding protein transpeptidase | ||||
Sequence: GALVAMDPHTGRVLAMVGGFSYAESEFNRATQAYRQPGSSFKPFVYAAALDNGYTPASVVLDGPLEINQGGSLGVWAPKNYSGKFSGPSTLRYGIEQSRNVMTVRLAQDMGMKLVAEYAERFGIYDKMLPVLSMALGAGETTVLRMVTAYSIIANGGQSITPSMVDRIQDRYGKTVFKHDNRQCEGCNAQDWANQDEPTLIDNRDQVLDPMTAYQITSMMEGVVQRGTAQILKSLDRPMAGKTGTTNDEKDAWFVGFTPDLVVGVFMGYDTPTSLGRGNTGGGLAAPVFKSFME | ||||||
Region | 796-819 | Disordered | ||||
Sequence: EGSPVAPQSPQATRAINSGSGGLY | ||||||
Compositional bias | 799-819 | Polar residues | ||||
Sequence: PVAPQSPQATRAINSGSGGLY |
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
- Length819
- Mass (Da)89,689
- Last updated2018-07-18 v1
- Checksum3AB1C80A7670AFD9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 799-819 | Polar residues | ||||
Sequence: PVAPQSPQATRAINSGSGGLY |