Table 1.

List of Fic domain containing proteins with known crystal structures. Modified from Truttmann & Ploegh [37] and Veyron et al. [38].

name	organism name	references	function/targets	structure (PDB ID)
IbpA	Histophilus somnii	[30,32,33]	AMPylation of Rho GTPases (Rac1, CDC42, RhoA-C, RhoG, TC10); cytotoxicity mediated by disruption of cytoskeletal regulation, repression of immune signalling pathways downstream of Rho GTPases	3N3U and 4ITR
VopS	Vibrio parahaemolyticus	[30,32,34]	AMPylation of Rho GTPases (CDC42, Rac1, RhoA, RhoG, TC10); cytotoxicity mediated by disruption of cytoskeletal regulation	3LET
AnkX	Legionella pneumophila	[4,39]	phospocholination of Rab1 and Rab35 GTPases; disrupts host cell endocyte recycling	4BEP, 4BER, 4BES and 4BET
DrrAb	Legionella pneumophila	[12,15]	AMPylation of GTPase Rab1b [14]; disrupts host intracellular vesicle transport and evades capture by lysosomes	3NKU, 3N6O, 3JZ9, 3JZA, 2WWX, 3L0I and 5O74
VbhT	Bartonella schenbuchensis	[40]	AMPylation of bacterial target of approximately 80 kDa; host target(s) unknown	3ZCB, 3ZC7 and 3SHG
GS-ATasea,b	E. coli	[41]	bifunctional enzyme; AMPylates and de-AMPylates bacterial glutamine synthetase through two distinct active sites	not available
EcFicT	Escherichia coli	[42]	host target(s) unknown; AMPylates bacterial type IIA topoisomerases and DNA gyrase; host target(s) unknown	5JFF and 5JFZ
YeFicT	Yersinia enterocolitica	[42]	AMPylates bacterial type IIA topoisomerases and DNA gyrase	not available
Bep1, Bep2	Bartonella rochalimae	[43–45]	Bep1 AMPylates Rac1/2/3 and RhoG, Bep2 AMPylates Vimentin; physiological function unknown	5EU0
NmFIC	Neisseria meningitidis	[46]	AMPylates endogenous DNA gyrase B; host targets unknown	2G03, 3S6A, 3SE5, 3SN9, 3ZLM,5CG7, 5CKL and 5CMT
HpFIC	Helicobacter pylori		physiological function unknown	2F6S
EfFIC	Enterococcus faecalis	[47]	host/endogenous targets unknown; possesses both AMPylation and de- AMPylation functions regulated by Ca2+ and Mg2+	5NUW, 5NV5, 6EP0, 6EP5, 6EP2, 5NWF and 5NVQ
BtFIC	Bacteroides thetaiotaomicron		physiological function unknown	3CUC
SoFIC	Shewanella oneidensis		physiological function unknown	3EQX, 3ZCN and 3ZEC
CdFIC	Clostridium difficile	[48]	unknown physiological targets; auto-AMPylates even in presence of inhibitory glutamate of the auto- inhibition motif	4X2E, 4X2C and 4X2D
HYPE	Homo sapiens	[49–53]	HYPEE234GAMPylates BiP, HSP70,HSP40, α-synuclein, eEF1A, E1F2AK2, H2-H4, ATP5A1, ATP5B, UBAP2 L, TUBB, CTSB,CTSC, CTSZ, ACP2, PNPLA3, ABHD6, TPP1, CAPZB and NSFL1C; involved in UPR activation in the ER, neuronal biogenesis, chaperone function modulation, altered aggregation of α-synuclein, ATP synthesis, cytoskeletal development and regulating protein translation	4U04, 4U0S, 4U07, 4U0U and 4U0Z
SelOb	Pseudomonas syringae	[54]	human orthologue regulates mitochondrial redox homeostasis through AMPylation of grxA and sucA	6EAC
dFICa	Drosophila melanogaster	[55–57]	AMPylates BiP; regulates stress response in ER, required for glia- specific histamine metabolism, neurotransmitter recycling, vision and maintenance of microvilli	crystal structure not available
FIC-1	Caenorhabditis elegans	[6,58]	AMPylates HSP1, HSP3 and eEF1- A2; involved in regulating sensitivity to pathogenic bacteria and modulating chaperone function in cytosol and ER	5JJ6 and 5JJ7
BeP	Bartonella quintana JK-31		physiological function unknown	4LU4
BepC	Bartonella henselae	[59]	triggers actin stress fibre formation in HeLa cells	4WGJ
BepA	Bartonella henselae	[60]	AMPylation of eukaryotic targets of approximately 40 kDa and 50 kDa; precise function unknown	5NH2, 2VZA, 2VY3 and 2JK8
Bep5	Bartonella claridgeiae		physiological function unknown	4XI8
Bep8	Bartonella sp.1–1c		physiological function unknown	4PY3
Dde2494	Desulfovibrio alaskensis		physiological function unknown	4RGL
AvrB	Pseudomonas synrigae	[61]	affects plant immunity by targeting RIN4 [62]; AMPylation activity unknown but can potentially act as an AMPylase	1NH1, 2NUD and 2NUN
PfhB2a	Pasteurella multocida	[7]	AMPylates Rho GTPases (CDC42, TC10, RhoA and Rac1); cytotoxicity mediated by disruption of cytoskeletal regulation	crystal structure of the PfhB2 Fic domain is unavailable

^aCrystal structures of dFIC, GS-ATase and the Fic domain of PfhB2 has not been solved.

^bGS-ATase, DrrA and SelO exhibit non-Fic-mediated AMPylation.