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Multifunctional virulence effector protein DrrA (Defects in Rab1 recruitment protein A) [Includes: Adenosine monophosphate-protein transferase (AMPylator) (EC 2.7.7.n1) (Guanosine monophosphate-protein transferase) (GMPylator) (EC 2.7.7.n6); Rab1 guanine nucleotide exchange factor]

 DRRA_LEGPN              Reviewed;         647 AA.
Q29ST3;
16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 1.
22-NOV-2017, entry version 44.
RecName: Full=Multifunctional virulence effector protein DrrA;
AltName: Full=Defects in Rab1 recruitment protein A;
Includes:
RecName: Full=Adenosine monophosphate-protein transferase;
Short=AMPylator;
EC=2.7.7.n1 {ECO:0000269|PubMed:20651120};
AltName: Full=Guanosine monophosphate-protein transferase;
Short=GMPylator;
EC=2.7.7.n6 {ECO:0000269|PubMed:20651120};
Includes:
RecName: Full=Rab1 guanine nucleotide exchange factor;
Name=drrA; Synonyms=sidM;
Legionella pneumophila.
Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
Legionellaceae; Legionella.
NCBI_TaxID=446;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A GUANINE NUCLEOTIDE
EXCHANGE FACTOR, AND SUBCELLULAR LOCATION.
STRAIN=130b / Wadsworth / Serogroup 1;
PubMed=16906144; DOI=10.1038/ncb1463;
Murata T., Delprato A., Ingmundson A., Toomre D.K., Lambright D.G.,
Roy C.R.;
"The Legionella pneumophila effector protein DrrA is a Rab1 guanine
nucleotide-exchange factor.";
Nat. Cell Biol. 8:971-977(2006).
[2]
FUNCTION.
PubMed=17952054; DOI=10.1038/nature06336;
Ingmundson A., Delprato A., Lambright D.G., Roy C.R.;
"Legionella pneumophila proteins that regulate Rab1 membrane
cycling.";
Nature 450:365-369(2007).
[3]
PTDINS(4)P-BINDING, DOMAIN P4M, AND SUBCELLULAR LOCATION.
STRAIN=JR32;
PubMed=19095644; DOI=10.1074/jbc.M807505200;
Brombacher E., Urwyler S., Ragaz C., Weber S.S., Kami K., Overduin M.,
Hilbi H.;
"Rab1 guanine nucleotide exchange factor SidM is a major
phosphatidylinositol 4-phosphate-binding effector protein of
Legionella pneumophila.";
J. Biol. Chem. 284:4846-4856(2009).
[4]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 9-218 IN COMPLEX WITH HOST
RAB1B, FUNCTION AS AN ADENOSINE MONOPHOSPHATE-PROTEIN TRANSFERASE,
CATALYTIC ACTIVITY, AND MUTAGENESIS OF 110-ASP--ASP-112.
PubMed=20651120; DOI=10.1126/science.1192276;
Muller M.P., Peters H., Blumer J., Blankenfeldt W., Goody R.S.,
Itzen A.;
"The Legionella effector protein DrrA AMPylates the membrane traffic
regulator Rab1b.";
Science 329:946-949(2010).
-!- FUNCTION: Virulence effector that plays a key role in hijacking
the host vesicular trafficking by recruiting the small guanosine
triphosphatase (GTPase) Rab1 to the cytosolic face of the
Legionella-containing vacuole (LCVs). Acts as a GDP-GTP exchange
factor (GEF) for the small GTPase Rab1 (RAB1A, RAB1B or RAB1C),
thereby converting Rab1 to an active GTP-bound state, leading to
the incorporation of Rab1 into LCVs. Also shows RabGDI
displacement factor (GDF) activity; however, this probably
represents a passive activity following the GEF activity. Also
acts as an adenylyltransferase by mediating the addition of
adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B,
thereby rendering RAB1B constitutively active. Also has
adenylyltransferase activity towards Rab6 and Rab35. Also displays
guanylyltransferase activity by mediating the addition of
guanosine 5'-monophosphate (GMP) to host RAB1B in vitro; however
such activity remains uncertain in vivo. Specifically binds
phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the
cytosolic surface of the phagosomal membrane shortly after
infection. {ECO:0000269|PubMed:16906144,
ECO:0000269|PubMed:17952054, ECO:0000269|PubMed:20651120}.
-!- CATALYTIC ACTIVITY: ATP + [protein]-L-tyrosine = diphosphate +
[protein]-O(4)-(5'-adenylyl)-L-tyrosine.
{ECO:0000269|PubMed:20651120}.
-!- CATALYTIC ACTIVITY: ATP + [protein]-L-threonine = diphosphate +
[protein]-O(4)-(5'-adenylyl)-L-threonine.
{ECO:0000269|PubMed:20651120}.
-!- CATALYTIC ACTIVITY: GTP + [protein]-L-tyrosine = diphosphate +
[protein]-O(4)-(5'-guanylyl)-L-tyrosine.
{ECO:0000269|PubMed:20651120}.
-!- INTERACTION:
P62820-1:RAB1A (xeno); NbExp=3; IntAct=EBI-15838677, EBI-15666813;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19095644}. Host
cytoplasmic vesicle membrane {ECO:0000269|PubMed:16906144};
Peripheral membrane protein {ECO:0000305|PubMed:16906144}.
Note=Translocated into the host cell via the type IV secretion
system (T4SS). Membrane association is mediated by PtdIns(4)P-
binding. {ECO:0000269|PubMed:19095644}.
-!- DOMAIN: The P4M (PtdIns(4)P-binding) region mediates binding to
PtdIns(4)P and membrane attachment. {ECO:0000269|PubMed:19095644}.
-!- SIMILARITY: Belongs to the DrrA family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY945933; AAY23285.1; -; Genomic_DNA.
RefSeq; WP_010948166.1; NZ_LT632616.1.
PDB; 3NKU; X-ray; 2.10 A; A/B=9-218.
PDB; 5O74; X-ray; 2.50 A; A/C/E/G/I/K=340-533.
PDBsum; 3NKU; -.
PDBsum; 5O74; -.
SMR; Q29ST3; -.
DIP; DIP-58604N; -.
IntAct; Q29ST3; 1.
PaxDb; Q29ST3; -.
EvolutionaryTrace; Q29ST3; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044161; C:host cell cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0044600; F:protein guanylyltransferase activity; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IDA:UniProtKB.
GO; GO:0009405; P:pathogenesis; IDA:UniProtKB.
GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
GO; GO:0018260; P:protein guanylylation; IDA:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
CDD; cd11689; SidM_DrrA_GEF; 1.
InterPro; IPR033784; DrrA_GEF.
InterPro; IPR028057; DrrA_P4M.
Pfam; PF14860; DrrA_P4M; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Guanine-nucleotide releasing factor;
Host cytoplasmic vesicle; Host membrane; Lipid-binding; Membrane;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Secreted; Transferase; Virulence.
CHAIN 1 647 Multifunctional virulence effector
protein DrrA.
/FTId=PRO_0000417544.
REGION 1 339 Adenosine monophosphate-protein
transferase.
REGION 340 520 Rab1 guanine nucleotide exchange factor.
REGION 544 647 P4M region.
MUTAGEN 110 112 DLD->ALA: Abolishes adenosine
monophosphate-protein transferase
activity. {ECO:0000269|PubMed:20651120}.
TURN 23 25 {ECO:0000244|PDB:3NKU}.
HELIX 31 53 {ECO:0000244|PDB:3NKU}.
HELIX 55 57 {ECO:0000244|PDB:3NKU}.
HELIX 61 84 {ECO:0000244|PDB:3NKU}.
STRAND 93 97 {ECO:0000244|PDB:3NKU}.
HELIX 100 102 {ECO:0000244|PDB:3NKU}.
HELIX 104 106 {ECO:0000244|PDB:3NKU}.
STRAND 112 116 {ECO:0000244|PDB:3NKU}.
HELIX 121 143 {ECO:0000244|PDB:3NKU}.
STRAND 157 161 {ECO:0000244|PDB:3NKU}.
HELIX 163 171 {ECO:0000244|PDB:3NKU}.
STRAND 175 177 {ECO:0000244|PDB:3NKU}.
HELIX 178 186 {ECO:0000244|PDB:3NKU}.
STRAND 189 193 {ECO:0000244|PDB:3NKU}.
HELIX 196 207 {ECO:0000244|PDB:3NKU}.
HELIX 211 214 {ECO:0000244|PDB:3NKU}.
SEQUENCE 647 AA; 73422 MW; DCE6EC98BCC3CDCA CRC64;
MSIMGRIKMS VNEEQFGSLY SDERDKPLLS PTAQKKFEEY QNKLANLSKI IRENEGNEVS
PWQEWENGLR QIYKEMIYDA FDALGVEMPK DMEVHFAGSL AKAQATEYSD LDAFVIVKND
EDIKKVKPVF DALNNLCQRI FTASNQIYPD PIGINPSRLI GTPDDLFGML KDGMVADVEA
TAMSILTSKP VLPRYELGEE LRDKIKQEPS FSNMVSAKKF YNKAIKDFTA PKEGAEVVSV
KTHIMRPIDF MLMGLREEFN LYSEDGAHLS APGTIRLLRE KNLLPEEQIA RIESVYNQAM
SKRFELHAEH KKEHDEMPYS DAKAMLDEVA KIRELGVQRV TRIENLENAK KLWDNANSML
EKGNISGYLK AANELHKFMK EKNLKEDDLR PELSDKTISP KGYAILQSLW GAASDYSRAA
ATLTESTVEP GLVSAVNKMS AFFMDCKLSP NERATPDPDF KVGKSKILVG IMQFIKDVAD
PTSKIWMHNT KALMNHKIAA IQKLERSNNV NDETLESVLS SKGENLSEYL SYKYATKDEG
REHRYTASTE NFKNVKEKYQ QMRGDALKTE ILADFKDKLA EATDEQSLKQ IVAELKSKDE
YRILAKGQGL TTQLLGLKTS SVSSFEKMVE ETRESIKSQE RQTIKIK


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