Amino acids
166
Annotations
8
Features
16
PDB binders
0
Overview
Basic information about this protein and its source genome.
- Accession
- PA3756
- Gene
- PA3756
- Status
- annotated
- Amino acids
- 166
- Structure source
- AlphaFold
GO
GO:0004180 Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain.
GO:0008234 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
GO:0071972 Catalysis of the reaction: 2 a peptidoglycan dimer (tetrapeptide) + 3 H2O = a peptidoglycan tetramer with L,D cross-links (L-Lys-D-Asn-L-Lys) + di-trans,poly-cis-undecaprenyl diphosphate + 4 D-alanine.
GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- Unknown
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
8 GO
Gene Ontology (GO)
8- GO:0004180 Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain.
- GO:0008234 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
- GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
- GO:0071972 Catalysis of the reaction: 2 a peptidoglycan dimer (tetrapeptide) + 3 H2O = a peptidoglycan tetramer with L,D cross-links (L-Lys-D-Asn-L-Lys) + di-trans,poly-cis-undecaprenyl diphosphate + 4 D-alanine.
- GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
- GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
- GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
- GO:0008360 Any process that modulates the surface configuration of a cell.
Sequence Features
Domain/signature hits from InterPro and related databases.
16 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 31 | 165 | CDD | cd16913 | YkuD_like |
| 31 | 165 | InterPro | IPR005490 | L,D-transpeptidase catalytic domain |
| 16 | 20 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 18 | 162 | PANTHER | PTHR36699 | LD-TRANSPEPTIDASE |
| 21 | 166 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 1 | 20 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 1 | 20 | SignalP_GRAM_NEGATIVE | SignalP-noTM | SignalP-noTM |
| 29 | 164 | Gene3D | G3DSA:2.40.440.10 | - |
| 29 | 164 | InterPro | IPR038063 | L,D-transpeptidase catalytic domain-like |
| 30 | 165 | SUPERFAMILY | SSF141523 | L,D-transpeptidase catalytic domain-like |
| 30 | 165 | InterPro | IPR038063 | L,D-transpeptidase catalytic domain-like |
| 1 | 3 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 31 | 164 | Pfam | PF03734 | L,D-transpeptidase catalytic domain |
| 31 | 164 | InterPro | IPR005490 | L,D-transpeptidase catalytic domain |
| 1 | 20 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 4 | 15 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
No pockets are loaded yet for the displayed AlphaFold model PA3756 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.
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Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA3756
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AlphaFold | — | — | full sequence | — | Viewing |