Protein profile

KP13_01689

Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase

Genome: KpKP13

Gene: AHE47003.1 wecA Structure source: AlphaFold + ColabFold UniProt A0A0H3GPT7

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Amino acids 367

Annotations 14

Features 43

PDB binders 0

Druggability 0.433

Overview

Basic information about this protein and its source genome.

Accession: KP13_01689
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE47003.1 wecA
Status: annotated
Amino acids: 367
Structure source: AlphaFold + ColabFold

2.7.8.33

GO:0009103 The chemical reactions and pathways resulting in the formation of lipopolysaccharides, any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria. GO:0016780 Catalysis of the transfer of a substituted phosphate group, other than diphosphate or nucleotidyl residues, from one compound (donor) to a another (acceptor). GO:0030145 Binding to a manganese ion (Mn). GO:0036380 Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0000287 Binding to a magnesium (Mg) ion.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 73.066
DEG E-value: 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 91.03

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.433

Structure A0A0H3GPT7

Pocket Pocket 32

P2Rank 0.841

Structure A0A0H3GPT7

Pocket Pocket 1

ColabFold model

FPocket 0.881 · Pocket 19

P2Rank 0.871 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 133 / 4744 genomes with a hit

Normalized 0.028

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Enzyme Commission (EC)

2.7.8.33

Gene Ontology (GO)

GO:0009103 The chemical reactions and pathways resulting in the formation of lipopolysaccharides, any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria.
GO:0016780 Catalysis of the transfer of a substituted phosphate group, other than diphosphate or nucleotidyl residues, from one compound (donor) to a another (acceptor).
GO:0030145 Binding to a manganese ion (Mn).
GO:0036380 Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0009276 The peptidoglycan layer of the Gram-negative cell envelope. In Gram-negative cells the peptidoglycan is relatively thin (1-2nm) and is linked to the outer membrane by lipoproteins. In Gram-negative cells the peptidoglycan is too thin to retain the primary stain in the Gram staining procedure and therefore cells appear red after Gram stain.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
GO:0044038 The chemical reactions and pathways resulting in the formation of a macromolecule destined to form part of a cell wall.
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:0009246 The chemical reactions and pathways resulting in the formation of the enterobacterial common antigen, an acidic polysaccharide containing N-acetyl-D-glucosamine, N-acetyl-D-mannosaminouronic acid, and 4-acetamido-4,6-dideoxy-D-galactose. A major component of the cell wall outer membrane of Gram-negative bacteria.
GO:0009243 The chemical reactions and pathways resulting in the formation of the O side chain of a lipopolysaccharide, which determines the antigenic specificity of the organism. It is made up of about 50 repeating units of a branched tetrasaccharide.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
72	89	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
40	289	CDD	cd06853	GT_WecA_like
8	350	NCBIfam	TIGR02380	UDP-N-acetylglucosamine--undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
8	350	InterPro	IPR012750	Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase
244	263	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
70	89	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
294	315	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	5	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
45	66	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
160	179	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
233	243	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
127	131	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
90	100	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
264	293	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
44	66	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
76	232	Pfam	PF00953	Glycosyl transferase family 4
76	232	InterPro	IPR000715	Glycosyl transferase, family 4
9	353	Hamap	MF_02030	Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase [wecA].
9	353	InterPro	IPR012750	Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase
180	184	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
242	261	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
185	202	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
3	312	PANTHER	PTHR22926	PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
3	312	InterPro	IPR000715	Glycosyl transferase, family 4
132	149	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
6	24	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
294	311	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
101	126	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
105	127	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
316	320	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
161	179	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
321	342	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
213	232	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
343	367	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
321	338	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
25	44	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
184	206	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
203	213	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
131	153	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
150	160	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
4	23	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
67	71	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
214	232	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GPT7	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01689	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
32				0.433
13				0.399

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	14.42	0.722
2	13.1	0.674
3	7.94	0.422
4	2.84	0.089
5	2.07	0.046

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
19				0.881
39				0.64

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	12.85	0.665
2	11.66	0.62
3	5.87	0.287
4	2.78	0.085
5	2.76	0.084

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

27 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

No PDB ligands found through similar proteins.

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL4286766	P0C1R8	10.80	946.0 Da LogP -6.69 TPSA 432.6	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4279378	P0C1R8	10.66	1156.3 Da LogP -1.58 TPSA 438.7	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4284923	P0C1R8	10.03	988.0 Da LogP -6.51 TPSA 435.7	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4475677	P0C1R8	8.59	784.0 Da LogP 0.71 TPSA 259.1	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCC[C@@H]1CN[C@@H]([C@H](O[C@@H]2…`
57M	Q03521	8.12	916.0 Da LogP -6.52 TPSA 425.9	3 viol.	✓ Clean	`CC(C)C[C@@H](C(=O)NCCCN[C@@H]([C@@H]([C@@H]1[C@…`
CHEMBL5265940	P0C1R8	7.77	583.6 Da LogP -4.18 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](n2ccc(=O)[nH]c2=O)O[C@@H…`
CHEMBL2048825	P0C1R8	7.66	711.7 Da LogP -1.68 TPSA 283.1	3 viol.	✓ Clean	`C[C@H](N)C(=O)N(C)[C@@H](C)[C@H](NC(=O)[C@H](C)…`
CHEMBL2048828	P0C1R8	7.66	876.9 Da LogP -2.67 TPSA 352.6	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL5272467	Q03521	7.66	726.7 Da LogP -2.74 TPSA 309.1	3 viol.	✓ Clean	`C[C@@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)…`
CHEMBL4473600	P0C1R8	7.62	711.9 Da LogP 0.66 TPSA 230.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)N[C@H]1CCN[C@H]([C@H](O[C@@…`
CHEMBL5277590	P0C1R8	7.57	473.4 Da LogP -4.18 TPSA 221.9	1 viol.	✓ Clean	`COC(=O)C1=C[C@@H](O)[C@@H](O)[C@H](O[C@@H](C(N)…`
CHEMBL2048826	P0C1R8	7.38	727.7 Da LogP -2.71 TPSA 303.3	3 viol.	✓ Clean	`C[C@H](N)C(=O)N(C)[C@@H](C)[C@H](NC(=O)[C@H](C)…`
CHEMBL5271984	Q03521	7.38	713.7 Da LogP -3.05 TPSA 312.1	3 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@@H](C)[C@H](NC(=O)[C@H](C)NC(…`
CHEMBL1780217	Q03521	7.31	916.0 Da LogP -6.31 TPSA 423.4	3 viol.	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](NC(=O)N[C@H](C(=O)O)C…`
CHEMBL2048830	P0C1R8	7.19	713.7 Da LogP -3.10 TPSA 303.3	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL1780218	Q03521	6.61	1070.3 Da LogP -1.88 TPSA 423.4	3 viol.	✓ Clean	`CCCCCCCCCCCCCCC[C@H](NC(=O)[C@@H](NC(=O)N[C@H](…`
9LH	P0C1R8	6.60	830.9 Da LogP -2.48 TPSA 311.8	3 viol.	✓ Clean	`CC(C)CCCCCCCCC/C=C/C(=O)N[C@@H]1[C@H]([C@H]([C@…`
CHEMBL5279603	P0C1R8	6.52	490.5 Da LogP -3.42 TPSA 215.5	2 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(N)cc2)[C@H]2O[…`
NKM	P0C1R8	6.48	569.5 Da LogP -4.57 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@H]([C@@H](O[C@@H]1[C@H](C(=O)N)O[C@@…`
CHEMBL5289885	P0C1R8	6.23	551.6 Da LogP -1.33 TPSA 189.5	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(-c3ccccc3)cc2)…`
CHEMBL2048831	P0C1R8	6.19	876.9 Da LogP -2.67 TPSA 352.6	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL5277496	P0C1R8	6.19	551.6 Da LogP -1.33 TPSA 189.5	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2cccc(-c3ccccc3)c2)…`
CHEMBL1780219	Q03521	6.16	1070.3 Da LogP -1.88 TPSA 423.4	3 viol.	✓ Clean	`CCCCCCCCCCCCCCC[C@@H](NC(=O)[C@@H](NC(=O)N[C@H]…`
CHEMBL5287014	P0C1R8	6.05	594.6 Da LogP -1.75 TPSA 218.6	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(C(=O)Nc3ccccc3…`
CHEMBL5268197	P0C1R8	6.02	630.6 Da LogP -2.20 TPSA 235.7	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2cccc(NS(=O)(=O)c3c…`
CHEMBL5291217	P0C1R8	6.00	630.6 Da LogP -2.20 TPSA 235.7	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(NS(=O)(=O)c3cc…`

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC34752870	0.500	257.2 Da LogP -2.23 TPSA 119.6	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](O)[C@@H](CN)O[C@H]1n1ccc(=O)[nH]…`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.