Protein profile

PA5117

regulatory protein TypA

Genome: NC_002516.2

Gene: bipA PA5117 typA Structure source: AlphaFold UniProt Q9HU67

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Amino acids 605

Annotations 17

Features 56

PDB binders 4

Druggability 0.237

Overview

Basic information about this protein and its source genome.

Accession: PA5117
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: bipA PA5117 typA
Status: annotated
Amino acids: 605
Structure source: AlphaFold

3.6.5.-

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:1990904 A macromolecular complex that contains both RNA and protein molecules. GO:0005525 Binding to GTP, guanosine triphosphate. GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. GO:0097216 Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions. GO:0043022 Binding to a ribosome.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 56.25
Human E-value: 9.52e-11
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: CytoplasmicMembrane

Selected Druggability evidence

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 0.237

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 16 GO

Enzyme Commission (EC)

3.6.5.-

Gene Ontology (GO)

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:1990904 A macromolecular complex that contains both RNA and protein molecules.
GO:0005525 Binding to GTP, guanosine triphosphate.
GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
GO:0097216 Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions.
GO:0043022 Binding to a ribosome.
GO:0019843 Binding to a ribosomal RNA.
GO:0000049 Binding to a transfer RNA.
GO:0071978 Bacterial-type flagellum-dependent cell motility in which the action of numerous flagella results in the smooth movement of a group of cells along a solid surface. Swarming motility is observed in groups of bacteria.
GO:0043709 The attachment of a cell to a solid substrate, via cell adhesion molecules, during the formation of a biofilm composed of microorganisms of the same species.
GO:0071236 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
GO:0010467 The process in which a gene's sequence is converted into a mature gene product (protein or RNA). This includes the production of an RNA transcript and its processing, as well as translation and maturation for protein-coding genes.
GO:0050714 Any process that activates or increases the frequency, rate or extent of the controlled release of a protein from a cell.
GO:0030254 The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
GO:0009409 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.
GO:0000027 The aggregation, arrangement and bonding together of constituent RNAs and proteins to form the large ribosomal subunit.

Sequence Features

Domain/signature hits from InterPro and related databases.

56 records

Show feature table

Start	End	DB	Term	Name
483	570	FunFam	G3DSA:2.40.50.250:FF:000001	GTP-binding protein TypA
151	299	SUPERFAMILY	SSF50447	Translation proteins
151	299	InterPro	IPR009000	Translation protein, beta-barrel domain superfamily
44	59	ProSitePatterns	PS00301	Translational (tr)-type guanine nucleotide-binding (G) domain signature.
44	59	InterPro	IPR031157	Tr-type G domain, conserved site
5	599	NCBIfam	TIGR01394	translational GTPase TypA/BipA
5	599	InterPro	IPR006298	GTP-binding protein BipA
200	598	PANTHER	PTHR42908	TRANSLATION ELONGATION FACTOR-RELATED
3	198	ProSiteProfiles	PS51722	Translational (tr)-type guanine nucleotide-binding (G) domain profile.
3	198	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
199	299	Gene3D	G3DSA:2.40.30.10	Translation factors
302	387	SUPERFAMILY	SSF54980	EF-G C-terminal domain-like
302	387	InterPro	IPR035647	EF-G domain III/V-like
4	195	Pfam	PF00009	Elongation factor Tu GTP binding domain
4	195	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
483	599	Gene3D	G3DSA:2.40.50.250	bipa protein
483	599	InterPro	IPR042116	GTP-binding protein TypA/BipA, C-terminal
3	601	Hamap	MF_00849	50S ribosomal subunit assembly factor BipA [bipA].
3	601	InterPro	IPR006298	GTP-binding protein BipA
219	289	Pfam	PF03144	Elongation factor Tu domain 2
219	289	InterPro	IPR004161	Translation elongation factor EFTu-like, domain 2
389	482	FunFam	G3DSA:3.30.70.240:FF:000002	GTP-binding protein TypA
5	134	NCBIfam	TIGR00231	small GTP-binding protein domain
5	134	InterPro	IPR005225	Small GTP-binding protein domain
32	52	Coils	Coil	Coil
3	219	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
3	219	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
306	420	FunFam	G3DSA:3.30.70.870:FF:000003	GTP-binding protein TypA
4	197	CDD	cd01891	TypA_BipA
4	197	InterPro	IPR047041	GTP-binding protein BipA, GTP-binding domain
199	299	FunFam	G3DSA:2.40.30.10:FF:000016	GTP-binding protein TypA
205	298	CDD	cd03691	BipA_TypA_II
205	298	InterPro	IPR047042	GTP-binding protein BipA, domain 2
398	476	CDD	cd03710	BipA_TypA_C
398	476	InterPro	IPR035651	BipA, domain V
397	477	Pfam	PF00679	Elongation factor G C-terminus
397	477	InterPro	IPR000640	Elongation factor EFG, domain V-like
306	590	Gene3D	G3DSA:3.30.70.870	Elongation Factor G (Translational Gtpase), domain 3
305	383	CDD	cd16263	BipA_III
305	383	InterPro	IPR047043	GTP-binding protein BipA, domain 3
1	198	Gene3D	G3DSA:3.40.50.300	-
1	198	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
389	482	Gene3D	G3DSA:3.30.70.240	-
398	512	SUPERFAMILY	SSF54980	EF-G C-terminal domain-like
398	512	InterPro	IPR035647	EF-G domain III/V-like
87	98	PRINTS	PR00315	GTP-binding elongation factor signature
87	98	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
51	59	PRINTS	PR00315	GTP-binding elongation factor signature
51	59	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
71	81	PRINTS	PR00315	GTP-binding elongation factor signature
71	81	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
7	20	PRINTS	PR00315	GTP-binding elongation factor signature
7	20	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
123	132	PRINTS	PR00315	GTP-binding elongation factor signature
123	132	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
1	198	FunFam	G3DSA:3.40.50.300:FF:000055	GTP-binding protein TypA

3D Structure

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

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Structural evidence

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA5117	AlphaFold	—	—	full sequence	—	Viewing

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
1				0.237
5				0.22

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.

54 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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
5MU	5J8B	Q5SKA7	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
G4P	4ZCM	P0A3B2	603.2 Da LogP -2.22 TPSA 345.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GCP	6U43	A0A062V290	521.2 Da LogP -2.22 TPSA 289.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GNP	2YWF	O67618	522.2 Da LogP -2.76 TPSA 301.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`

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).

No ChEMBL hits found through similar proteins.

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
ZINC13515793	1.000	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]2…`
ZINC104869865	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC13518650	0.837	418.2 Da LogP -2.31 TPSA 217.8	1 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[C…`
ZINC13519607	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)OP…`
ZINC31298140	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168754	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168756	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC12501413	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496	0.783	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC13518175	0.755	450.1 Da LogP -2.13 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC205346095	0.698	369.2 Da LogP -2.83 TPSA 214.4	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC71774763	0.681	432.3 Da LogP -2.23 TPSA 198.3	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@](=O)(O)N3CCOCC3…`
ZINC2046807	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)[n…`
ZINC2125635	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O)[…`
ZINC21999938	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)[n…`
ZINC2583634	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)[n…`
ZINC4028557	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[nH…`
ZINC4557135	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)[n…`
ZINC4557136	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)[…`
ZINC4557137	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC5765081	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)[…`
ZINC4602228	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@H]2…`
ZINC4602229	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@H]…`
ZINC4602233	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@@H]…`
ZINC4602235	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@@H…`
ZINC4743771	0.662	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4743772	0.662	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC4743774	0.662	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4743775	0.662	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC12503703	0.647	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC12503831	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC12503833	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC1532538	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC2123545	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC36377965	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC8215878	0.647	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC9235501	0.647	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H…`

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.