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Literature summary extracted from

  • Truttmann, M.; Ploegh, H.
    rAMPing up stress signaling Protein AMPylation in Metazoans (2017), Trends Cell Biol., 27, 608-620 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.108 E274G animals that express the constitutively active Fic (E274G) mutant show enhanced tolerance to the Pseudomonas aeruginosa Caenorhabditis elegans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.108 cytoplasm
-
 Caenorhabditis elegans 5737
-
2.7.7.108 endoplasmic reticulum
-
 Drosophila melanogaster 5783
-
2.7.7.108 endoplasmic reticulum the enzyme predominantly localizes to the ER-nuclear envelope continuum Caenorhabditis elegans 5783
-
2.7.7.108 extracellular
-
 Legionella pneumophila
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.108 Ca2+ the enzyme AMPylates the endoplasmic reticulum-resident HSP70 chaperone Grp78/BiP in a Ca2+-dependent manner Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.108 ATP + [CDC42]-L-tyrosine Histophilus somni
-
 diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
 ?
2.7.7.108 ATP + [CDC42]-L-tyrosine Histophilus somni 2336
-
 diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
 ?
2.7.7.108 ATP + [Hsp-3]-L-threonine Caenorhabditis elegans Hsp-3 is AMPylated on Thr176 diphosphate + [Hsp-3]-O-(5'-adenylyl)-L-threonine
-
 ?
2.7.7.108 ATP + [HSP70 chaperone Grp78/BiP]-L-threonine Drosophila melanogaster the modified site is Thr366 diphosphate + [HSP70 chaperone Grp78/BiP]-O-(5'-adenylyl)-L-threonine
-
 ?
2.7.7.108 ATP + [pRab1]-L-tyrosine Legionella pneumophila AMPylates Rab1 on Tyr77 diphosphate + [pRab1]-O-(5'-adenylyl)-L-tyrosine
-
 ?
2.7.7.108 ATP + [Rho]-L-threonine Vibrio parahaemolyticus modifies Thr35 in the switch I loop of small Rho GTPase diphosphate + [Rho]-O-(5'-adenylyl)-L-threonine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.108 Caenorhabditis elegans Q23544
-
-
2.7.7.108 Drosophila melanogaster Q8SWV6
-
-
2.7.7.108 Histophilus somni Q06277
-
-
2.7.7.108 Histophilus somni 2336 Q06277
-
-
2.7.7.108 Legionella pneumophila Q29ST3
-
-
2.7.7.108 Pasteurella multocida
-
-
-
2.7.7.108 Vibrio parahaemolyticus Q87P32 serotype O3:K6
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.7.108 glycoprotein N-glycosylated on Asn288 Drosophila melanogaster
2.7.7.108 proteolytic modification the enzyme is proteolytically processed Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.108 ATP + [CDC42]-L-tyrosine
-
 Histophilus somni diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
 ?
2.7.7.108 ATP + [CDC42]-L-tyrosine
-
 Histophilus somni 2336 diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
 ?
2.7.7.108 ATP + [Hsp-3]-L-threonine Hsp-3 is AMPylated on Thr176 Caenorhabditis elegans diphosphate + [Hsp-3]-O-(5'-adenylyl)-L-threonine
-
 ?
2.7.7.108 ATP + [HSP70 chaperone Grp78/BiP]-L-threonine the modified site is Thr366 Drosophila melanogaster diphosphate + [HSP70 chaperone Grp78/BiP]-O-(5'-adenylyl)-L-threonine
-
 ?
2.7.7.108 ATP + [pRab1]-L-tyrosine AMPylates Rab1 on Tyr77 Legionella pneumophila diphosphate + [pRab1]-O-(5'-adenylyl)-L-tyrosine
-
 ?
2.7.7.108 ATP + [Rho]-L-threonine modifies Thr35 in the switch I loop of small Rho GTPase Vibrio parahaemolyticus diphosphate + [Rho]-O-(5'-adenylyl)-L-threonine
-
 ?
2.7.7.108 additional information AMPylation of human HSP40 and HSP70 as well as HSP-1 (in vitro) and Ssa2 (both in vitro and in vivo) is attributed to Fic-1 (E274G) activity Caenorhabditis elegans ?
-
-
2.7.7.108 additional information the enzyme transfers AMP to Rho, Rac1 and Cdc42 Pasteurella multocida ?
-
-

Synonyms

EC Number Synonyms Comment Organism
2.7.7.108 CG9523
-
 Drosophila melanogaster
2.7.7.108 DrrA
-
 Legionella pneumophila
2.7.7.108 FIC-1
-
 Caenorhabditis elegans
2.7.7.108 IbpA
-
 Histophilus somni
2.7.7.108 PfhB2
-
 Pasteurella multocida
2.7.7.108 SidM
-
 Legionella pneumophila
2.7.7.108 VopS
-
 Vibrio parahaemolyticus

Expression

EC Number Organism Comment Expression
2.7.7.108 Caenorhabditis elegans the enzyme is expressed at low levels throughout the worm body, but is most pronounced in the adult germline and in embryonic cells up

General Information

EC Number General Information Comment Organism
2.7.7.108 malfunction Fic-1 knock-out worms are more susceptible to infection by Pseudomonas aeruginosa Caenorhabditis elegans
2.7.7.108 malfunction knock-out flies are insensitive to light stimuli due to a failure to activate postsynaptic neurons Drosophila melanogaster
2.7.7.108 physiological function AMPylation of Rab1b restricts binding of GTPase activating proteins (GAPs) and subsequent activation of Rab1b, thus locking Rab1b in the GTP-bound state. Simultaneously, AMPylation of Rab1b blocks downstream interactions with binding partners such as MICAL-3 and enhances retention of Rab1b at Legionella-containing vacuoles (LCVs) during infection Legionella pneumophila
2.7.7.108 physiological function limited role for Fic-1 mediated AMPylation in the regulation of endoplasmic reticulum homeostasis Caenorhabditis elegans
2.7.7.108 physiological function protein AMPylation, the covalent attachment of an adenosine 5'-monophosphate (AMP) residue to amino acid side chains using ATP as the donor, is a post-translational modification that is relevant for both normal and pathological cell signaling. In metazoans, single copies of fic-domain-containing AMPylases, the enzymes responsible for AMPylation, preferentially modify a set of dedicated targets and contribute to the perception of cellular stress and its regulation. Pathogenic bacteria can exploit AMPylation of eukaryotic target proteins to rewire host cell signaling machinery in support of their propagation and survival Vibrio parahaemolyticus
2.7.7.108 physiological function VopS-mediated AMPylation of Rho, Rac1 and Cdc42 impairs cellular signaling in several ways. The AMP moiety interferes with the binding of direct interaction partners, and also prevents E3 ubiquitin ligases from targeting these now non-functional AMPylated GTPases for proteolytic degradation. VopS also alters cellular immunity through inhibition of the pro-inflammatory NFkappaB signaling cascade, limits the generation of superoxide and attenuates Erk and JNK signaling. AMPylation of Rho GTPases further activates the pyrin-dependent inflammasome while inhibiting NLRC4-dependent inflammasome activation. As a direct consequence, the actin cytoskeleton collapses and cells rapidly die Vibrio parahaemolyticus