eta

Functionⁱ

An NAD-dependent ADP-ribosyltransferase (ADPRT). Catalyzes the transfer of the ADP ribosyl moiety of oxidized NAD (NAD⁺) onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. Has an LD₅₀ of 65 ng/ml against the human lung epithelial cell line C38.1 Publication

Catalytic activityⁱ

NAD⁺ + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2].

Activity regulationⁱ

Inhibited by 1,8-naphthalimide (NAP) as well as a number of poly(ADP-ribose) polymerase inhibitors and other compounds.1 Publication

Kineticsⁱ

For ADP-ribosyltransferase activity of the catalytic fragment 399-605.

K_M=121 µM for NAD

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	474	NAD1 Publication	1
Active siteⁱ	578	1 Publication	1
Binding siteⁱ	578	NAD1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	465 – 467	NAD1 Publication		3
Nucleotide bindingⁱ	479 – 485	NAD1 Publication		7

GO - Molecular functionⁱ

NAD+-diphthamide ADP-ribosyltransferase activity
Source: CACAO
Inferred from direct assayⁱ
- 2170123
toxin activity Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosyltransferase, Toxin, Transferase
Ligand	NAD

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-15587 PAER208964:G1FZ6-1174-MONOMER
BRENDAⁱ	2.4.2.36 5087
SABIO-RKⁱ	P11439

Protein family/group databases

TCDBⁱ	1.C.73.1.1 the pseudomonas exotoxin a (p-exoa) family

TCDBⁱ

1.C.73.1.1 the pseudomonas exotoxin a (p-exoa) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Exotoxin A (EC:2.4.2.36) Short name: ETA Alternative name(s): NAD(+)--diphthamide ADP-ribosyltransferase PE
Gene namesⁱ	Name:eta Ordered Locus Names:PA1148
Organismⁱ	Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifierⁱ	208964 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa
Proteomesⁱ	UP000002438 Componentⁱ: Chromosome

Organism-specific databases

Pseudomonas genome database More...PseudoCAPⁱ	PA1148

PseudoCAPⁱ

PA1148

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	82	K → E: Loss of toxicity, no binding to LRP1 receptor. 1 Publication	1
Mutagenesisⁱ	481	R → H: 52-fold decrease in ADPRT activity, 55-fold reduction in GH activity, 31-fold increase in dissociation constant for NAD(+). 1 Publication	1
Mutagenesisⁱ	571	E → A: 833-fold decrease in ADPRT activity, 4-fold reduction in GH activity, 2-fold increase in dissociation constant for NAD(+). 1 Publication	1
Mutagenesisⁱ	576	R → A: 2-fold decrease in ADPRT activity, 14-fold reduction in GH activity, 3-fold increase in dissociation constant for NAD(+). 1 Publication	1
Mutagenesisⁱ	578	E → A: 666-fold decrease in ADPRT activity, 14-fold reduction in GH activity, 2-fold increase in dissociation constant for NAD(+), loss of toxicity against mouse cells. 2 Publications	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB02701 Nicotinamide

DrugBankⁱ

DB02701 Nicotinamide

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 25	1 PublicationAdd BLAST		25
ChainⁱPRO_0000019365	26 – 638	Exotoxin AAdd BLAST		613

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Disulfide bondⁱ	290 ↔ 312	1 Publication

Post-translational modificationⁱ

The 8 cysteines participate in intrachain disulfide bonds.

Keywords - PTMⁱ

Disulfide bond

Proteomic databases

PaxDbⁱ	P11439
PRIDEⁱ	P11439

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	208964.PA1148

STRINGⁱ

208964.PA1148

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	32 – 35	Combined sources	4
Beta strandⁱ	36 – 43	Combined sources	8
Beta strandⁱ	49 – 54	Combined sources	6
Helixⁱ	57 – 60	Combined sources	4
Beta strandⁱ	63 – 74	Combined sources	12
Turnⁱ	76 – 79	Combined sources	4
Beta strandⁱ	80 – 85	Combined sources	6
Turnⁱ	86 – 88	Combined sources	3
Beta strandⁱ	89 – 93	Combined sources	5
Beta strandⁱ	95 – 102	Combined sources	8
Beta strandⁱ	106 – 108	Combined sources	3
Beta strandⁱ	110 – 115	Combined sources	6
Beta strandⁱ	117 – 120	Combined sources	4
Beta strandⁱ	122 – 131	Combined sources	10
Beta strandⁱ	136 – 145	Combined sources	10
Beta strandⁱ	151 – 154	Combined sources	4
Beta strandⁱ	157 – 161	Combined sources	5
Helixⁱ	164 – 170	Combined sources	7
Beta strandⁱ	173 – 180	Combined sources	8
Beta strandⁱ	189 – 201	Combined sources	13
Helixⁱ	213 – 216	Combined sources	4
Helixⁱ	218 – 223	Combined sources	6
Helixⁱ	225 – 227	Combined sources	3
Helixⁱ	230 – 235	Combined sources	6
Helixⁱ	243 – 246	Combined sources	4
Beta strandⁱ	249 – 255	Combined sources	7
Beta strandⁱ	270 – 273	Combined sources	4
Helixⁱ	280 – 290	Combined sources	11
Helixⁱ	294 – 298	Combined sources	5
Helixⁱ	307 – 311	Combined sources	5
Helixⁱ	313 – 325	Combined sources	13
Helixⁱ	330 – 332	Combined sources	3
Helixⁱ	333 – 342	Combined sources	10
Turnⁱ	344 – 347	Combined sources	4
Helixⁱ	348 – 356	Combined sources	9
Helixⁱ	358 – 376	Combined sources	19
Helixⁱ	384 – 387	Combined sources	4
Beta strandⁱ	392 – 396	Combined sources	5
Beta strandⁱ	399 – 403	Combined sources	5
Helixⁱ	408 – 410	Combined sources	3
Beta strandⁱ	413 – 418	Combined sources	6
Helixⁱ	422 – 424	Combined sources	3
Beta strandⁱ	428 – 430	Combined sources	3
Beta strandⁱ	433 – 435	Combined sources	3
Beta strandⁱ	438 – 440	Combined sources	3
Helixⁱ	444 – 456	Combined sources	13
Beta strandⁱ	459 – 467	Combined sources	9
Helixⁱ	469 – 477	Combined sources	9
Helixⁱ	489 – 491	Combined sources	3
Beta strandⁱ	493 – 499	Combined sources	7
Helixⁱ	500 – 504	Combined sources	5
Beta strandⁱ	522 – 529	Combined sources	8
Helixⁱ	530 – 535	Combined sources	6
Beta strandⁱ	536 – 538	Combined sources	3
Beta strandⁱ	543 – 545	Combined sources	3
Helixⁱ	548 – 556	Combined sources	9
Beta strandⁱ	558 – 561	Combined sources	4
Beta strandⁱ	566 – 572	Combined sources	7
Beta strandⁱ	577 – 581	Combined sources	5
Helixⁱ	583 – 587	Combined sources	5
Beta strandⁱ	590 – 593	Combined sources	4
Helixⁱ	609 – 611	Combined sources	3
Helixⁱ	614 – 617	Combined sources	4
Beta strandⁱ	626 – 628	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P11439
SMRⁱ	P11439
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P11439

EvolutionaryTraceⁱ

P11439

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	26 – 277	IA (required for target cell recognition)Add BLAST	252
Regionⁱ	278 – 389	II (required for translocation in target cell cytoplasm)Add BLAST	112
Regionⁱ	390 – 429	IBAdd BLAST	40
Regionⁱ	430 – 638	III (required for ADP-ribosyl activity)Add BLAST	209

Keywords - Domainⁱ

Signal

Phylogenomic databases

HOGENOMⁱ	HOG000081585
KEGG Orthology (KO) More...KOⁱ	K11020
OMAⁱ	HESNEMQ

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01436 Dipth_tox_like, 1 hit
Gene3Dⁱ	3.90.1350.10, 1 hit
InterProⁱ	View protein in InterPro IPR013320 ConA-like_dom_sf IPR015185 Exotox-A_bind IPR015099 Exotox-A_cataly_dom IPR015186 Exotox-A_middle_dom IPR036478 Exotox-A_middle_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF09101 Exotox-A_bind, 1 hit PF09009 Exotox-A_cataly, 1 hit PF09102 Exotox-A_target, 1 hit
SUPFAMⁱ	SSF49899 SSF49899, 1 hit SSF56864 SSF56864, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P11439-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MHLTPHWIPL VASLGLLAGG SFASAAEEAF DLWNECAKAC VLDLKDGVRS 
        60         70         80         90        100
SRMSVDPAIA DTNGQGVLHY SMVLEGGNDA LKLAIDNALS ITSDGLTIRL 
       110        120        130        140        150
EGGVEPNKPV RYSYTRQARG SWSLNWLVPI GHEKPSNIKV FIHELNAGNQ 
       160        170        180        190        200
LSHMSPIYTI EMGDELLAKL ARDATFFVRA HESNEMQPTL AISHAGVSVV 
       210        220        230        240        250
MAQAQPRREK RWSEWASGKV LCLLDPLDGV YNYLAQQRCN LDDTWEGKIY 
       260        270        280        290        300
RVLAGNPAKH DLDIKPTVIS HRLHFPEGGS LAALTAHQAC HLPLETFTRH 
       310        320        330        340        350
RQPRGWEQLE QCGYPVQRLV ALYLAARLSW NQVDQVIRNA LASPGSGGDL 
       360        370        380        390        400
GEAIREQPEQ ARLALTLAAA ESERFVRQGT GNDEAGAASA DVVSLTCPVA 
       410        420        430        440        450
AGECAGPADS GDALLERNYP TGAEFLGDGG DISFSTRGTQ NWTVERLLQA 
       460        470        480        490        500
HRQLEERGYV FVGYHGTFLE AAQSIVFGGV RARSQDLDAI WRGFYIAGDP 
       510        520        530        540        550
ALAYGYAQDQ EPDARGRIRN GALLRVYVPR SSLPGFYRTG LTLAAPEAAG 
       560        570        580        590        600
EVERLIGHPL PLRLDAITGP EEEGGRLETI LGWPLAERTV VIPSAIPTDP 
       610        620        630 
RNVGGDLDPS SIPDKEQAIS ALPDYASQPG KPPREDLK

Length:638

Mass (Da):69,284

Last modified:January 11, 2001 - v2

Checksum:ⁱ7B9AAD56A27C700A

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	4	T → I in AAB59097 (PubMed:6201861).Curated	1
Sequence conflictⁱ	22	F → S in AAB59097 (PubMed:6201861).Curated	1
Sequence conflictⁱ	204	A → T in AAB59097 (PubMed:6201861).Curated	1
Sequence conflictⁱ	389	S → N in AAB59097 (PubMed:6201861).Curated	1
Sequence conflictⁱ	432	I → V in AAB59097 (PubMed:6201861).Curated	1
Sequence conflictⁱ	540	G → S in AAB59097 (PubMed:6201861).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	K01397 Genomic DNA Translation: AAB59097.1 AE004091 Genomic DNA Translation: AAG04537.1
PIRⁱ	A30347 C83503
NCBI Reference Sequences More...RefSeqⁱ	NP_249839.1, NC_002516.2 WP_003112478.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaⁱ	AAG04537; AAG04537; PA1148
GeneIDⁱ	877850
KEGGⁱ	pae:PA1148
PATRICⁱ	fig\|208964.12.peg.1194

Protein	Similar proteins		Species	Score	Length	Source
P11439	Exotoxin A		PSEAI		638	UniRef90_P11439
Exotoxin		Pseudomonas sp. HMSC059F05		638
Exotoxin A		Pseudomonas aeruginosa BL04		638
Exotoxin A		Pseudomonas aeruginosa MH27		638
Exotoxin		Pseudomonas sp. HMSC065H01		638
+304

Protein	Similar proteins		Species	Score	Length	Source
P11439	Exotoxin		PSEAI		638	UniRef50_P11439
Exotoxin A		Pseudomonas aeruginosa BL04		638
Exotoxin A		Pseudomonas aeruginosa MH27		638
Exotoxin		Pseudomonas sp. HMSC065H01		638
Exotoxin		Pseudomonas sp. HMSC059F05		638
+340

Entry informationⁱ

Entry nameⁱ	TOXA_PSEAE
Accessionⁱ	P11439Primary (citable) accession number: P11439 Secondary accession number(s): Q9I4I7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
	Last sequence update:	January 11, 2001
	Last modified:	September 12, 2018
	This is version 140 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P11439 (TOXA_PSEAE)

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Exotoxin A

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi