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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_LEGPH              Reviewed;         647 AA.
Q5ZSQ3;
16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
23-MAY-2018, entry version 73.
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;
AltName: Full=Guanosine monophosphate-protein transferase;
Short=GMPylator;
EC=2.7.7.n6;
Includes:
RecName: Full=Rab1 guanine nucleotide exchange factor;
Name=drrA; Synonyms=sidM; OrderedLocusNames=lpg2464;
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 /
ATCC 33152 / DSM 7513).
Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
Legionellaceae; Legionella.
NCBI_TaxID=272624;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS A GUANINE NUCLEOTIDE EXCHANGE
FACTOR, AND SUBCELLULAR LOCATION.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=16824952; DOI=10.1016/j.devcel.2006.05.013;
Machner M.P., Isberg R.R.;
"Targeting of host Rab GTPase function by the intravacuolar pathogen
Legionella pneumophila.";
Dev. Cell 11:47-56(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=15448271; DOI=10.1126/science.1099776;
Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M.,
Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J.,
Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R.,
Pampou S., Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E.,
Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G.,
Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J.,
Ju J., Kalachikov S., Shuman H.A., Russo J.J.;
"The genomic sequence of the accidental pathogen Legionella
pneumophila.";
Science 305:1966-1968(2004).
[3]
FUNCTION.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=17947549; DOI=10.1126/science.1149121;
Machner M.P., Isberg R.R.;
"A bifunctional bacterial protein links GDI displacement to Rab1
activation.";
Science 318:974-977(2007).
[4]
FUNCTION.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=21822290; DOI=10.1038/nature10335;
Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
"Modulation of Rab GTPase function by a protein phosphocholine
transferase.";
Nature 477:103-106(2011).
[5]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 340-533, FUNCTION, AND
MUTAGENESIS OF 451-ASN--ARG-453; ASP-480 AND SER-483.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=20064470; DOI=10.1016/j.molcel.2009.11.014;
Schoebel S., Oesterlin L.K., Blankenfeldt W., Goody R.S., Itzen A.;
"RabGDI displacement by DrrA from Legionella is a consequence of its
guanine nucleotide exchange activity.";
Mol. Cell 36:1060-1072(2009).
[6]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 317-533, FUNCTION,
INTERACTION WITH HOST RAB1A, AND MUTAGENESIS OF ALA-435.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=19942850; DOI=10.1038/emboj.2009.347;
Suh H.Y., Lee D.W., Lee K.H., Ku B., Choi S.J., Woo J.S., Kim Y.G.,
Oh B.H.;
"Structural insights into the dual nucleotide exchange and GDI
displacement activity of SidM/DrrA.";
EMBO J. 29:496-504(2010).
[7]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 193-550, FUNCTION,
INTERACTION WITH HOST RAB1A, AND MUTAGENESIS OF TRP-410; GLY-431;
ALA-435; 451-ASN--ARG-453; ARG-541; LYS-568 AND THR-619.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=20176951; DOI=10.1073/pnas.0914231107;
Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F.;
"Structural mechanism of host Rab1 activation by the bifunctional
Legionella type IV effector SidM/DrrA.";
Proc. Natl. Acad. Sci. U.S.A. 107:4699-4704(2010).
[8]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 340-647, AND
PTDINS(4)P-BINDING.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=20616805; DOI=10.1038/embor.2010.97;
Schoebel S., Blankenfeldt W., Goody R.S., Itzen A.;
"High-affinity binding of phosphatidylinositol 4-phosphate by
Legionella pneumophila DrrA.";
EMBO Rep. 11:598-604(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:16824952,
ECO:0000269|PubMed:17947549, ECO:0000269|PubMed:19942850,
ECO:0000269|PubMed:20064470, ECO:0000269|PubMed:20176951,
ECO:0000269|PubMed:21822290}.
-!- CATALYTIC ACTIVITY: ATP + [protein]-L-tyrosine = diphosphate +
[protein]-O(4)-(5'-adenylyl)-L-tyrosine.
-!- CATALYTIC ACTIVITY: ATP + [protein]-L-threonine = diphosphate +
[protein]-O(4)-(5'-adenylyl)-L-threonine.
-!- CATALYTIC ACTIVITY: GTP + [protein]-L-tyrosine = diphosphate +
[protein]-O(4)-(5'-guanylyl)-L-tyrosine.
-!- SUBUNIT: Interacts with host RAB1A. {ECO:0000269|PubMed:19942850,
ECO:0000269|PubMed:20176951}.
-!- INTERACTION:
P62820:RAB1A (xeno); NbExp=7; IntAct=EBI-7632432, EBI-716845;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16824952}. Host
cytoplasmic vesicle membrane {ECO:0000269|PubMed:16824952};
Peripheral membrane protein {ECO:0000269|PubMed:16824952}.
Note=Translocated into the host cell via the type IV secretion
system (T4SS). Membrane association is mediated by PtdIns(4)P-
binding.
-!- DOMAIN: The P4M (PtdIns(4)P-binding) region mediates binding to
PtdIns(4)P and membrane attachment. {ECO:0000250}.
-!- SIMILARITY: Belongs to the DrrA family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; DQ845395; ABG90503.1; -; mRNA.
EMBL; AE017354; AAU28524.1; -; Genomic_DNA.
RefSeq; WP_010948166.1; NC_002942.5.
RefSeq; YP_096471.1; NC_002942.5.
PDB; 2WWX; X-ray; 1.50 A; B=317-533.
PDB; 3JZ9; X-ray; 1.80 A; A=340-533.
PDB; 3JZA; X-ray; 1.80 A; B=340-533.
PDB; 3L0I; X-ray; 2.85 A; A/C=193-550.
PDB; 3L0M; X-ray; 3.45 A; A/B=317-647.
PDB; 3N6O; X-ray; 2.50 A; A/B=340-647.
PDB; 4MXP; X-ray; 1.83 A; A=330-647.
PDBsum; 2WWX; -.
PDBsum; 3JZ9; -.
PDBsum; 3JZA; -.
PDBsum; 3L0I; -.
PDBsum; 3L0M; -.
PDBsum; 3N6O; -.
PDBsum; 4MXP; -.
SMR; Q5ZSQ3; -.
IntAct; Q5ZSQ3; 1.
MINT; Q5ZSQ3; -.
STRING; 272624.lpg2464; -.
PaxDb; Q5ZSQ3; -.
PRIDE; Q5ZSQ3; -.
EnsemblBacteria; AAU28524; AAU28524; lpg2464.
GeneID; 19834029; -.
KEGG; lpn:lpg2464; -.
PATRIC; fig|272624.6.peg.2613; -.
HOGENOM; HOG000126893; -.
KO; K15480; -.
OMA; AQATEYS; -.
EvolutionaryTrace; Q5ZSQ3; -.
Proteomes; UP000000609; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044161; C:host cell cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IEA:GOC.
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; ISS: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; ISS:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
GO; GO:0009405; P:pathogenesis; ISS:UniProtKB.
GO; GO:0018117; P:protein adenylylation; ISS:UniProtKB.
GO; GO:0018260; P:protein guanylylation; ISS:UniProtKB.
GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
CDD; cd11689; SidM_DrrA_GEF; 1.
Gene3D; 1.20.1280.280; -; 1.
InterPro; IPR033784; DrrA_GEF.
InterPro; IPR028057; DrrA_P4M.
InterPro; IPR038346; DrrA_PI4P-bd_sf.
Pfam; PF14860; DrrA_P4M; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Guanine-nucleotide releasing factor; Host cytoplasmic vesicle;
Host membrane; Lipid-binding; Membrane; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
Secreted; Transferase; Virulence.
CHAIN 1 647 Multifunctional virulence effector
protein DrrA.
/FTId=PRO_0000417545.
REGION 1 339 Adenosine monophosphate-protein
transferase.
REGION 340 520 Rab1 guanine nucleotide exchange factor.
REGION 544 647 P4M region.
MUTAGEN 410 410 W->D: Almost abolishes GEF and GDF
activities, but still binds Rab1.
{ECO:0000269|PubMed:20176951}.
MUTAGEN 431 431 G->D: Abolishes GEF and GDF activities,
but still binds Rab1.
{ECO:0000269|PubMed:20176951}.
MUTAGEN 435 435 A->D,E: Abolishes GEF and GDF activities,
but still binds Rab1.
{ECO:0000269|PubMed:19942850,
ECO:0000269|PubMed:20176951}.
MUTAGEN 451 453 NER->AEA: Almost abolishes GEF and GDF
activities, with a more severe effect on
GEF activity.
{ECO:0000269|PubMed:20064470,
ECO:0000269|PubMed:20176951}.
MUTAGEN 480 480 D->A: Slightly impairs GEF and GDF
activities; when associated with A-483.
{ECO:0000269|PubMed:20064470}.
MUTAGEN 483 483 S->A: Slightly impairs GEF and GDF
activities; when associated with A-480.
{ECO:0000269|PubMed:20064470}.
MUTAGEN 541 541 R->A: Abolishes PtdIns(4)P-binding; when
associated with A-568.
{ECO:0000269|PubMed:20176951}.
MUTAGEN 568 568 K->A: Abolishes PtdIns(4)P-binding; when
associated with A-541 or A-619.
{ECO:0000269|PubMed:20176951}.
MUTAGEN 619 619 T->A: Abolishes PtdIns(4)P-binding; when
associated with A-568.
{ECO:0000269|PubMed:20176951}.
HELIX 214 224 {ECO:0000244|PDB:3L0I}.
HELIX 240 243 {ECO:0000244|PDB:3L0I}.
HELIX 245 258 {ECO:0000244|PDB:3L0I}.
HELIX 271 280 {ECO:0000244|PDB:3L0I}.
HELIX 286 307 {ECO:0000244|PDB:3L0I}.
HELIX 320 322 {ECO:0000244|PDB:3L0I}.
HELIX 336 361 {ECO:0000244|PDB:2WWX}.
HELIX 365 381 {ECO:0000244|PDB:2WWX}.
HELIX 386 389 {ECO:0000244|PDB:2WWX}.
HELIX 390 393 {ECO:0000244|PDB:2WWX}.
HELIX 400 419 {ECO:0000244|PDB:2WWX}.
HELIX 428 447 {ECO:0000244|PDB:2WWX}.
STRAND 450 452 {ECO:0000244|PDB:3JZ9}.
HELIX 458 460 {ECO:0000244|PDB:3JZA}.
HELIX 464 478 {ECO:0000244|PDB:2WWX}.
HELIX 490 506 {ECO:0000244|PDB:2WWX}.
HELIX 512 520 {ECO:0000244|PDB:2WWX}.
STRAND 526 528 {ECO:0000244|PDB:3JZ9}.
TURN 530 533 {ECO:0000244|PDB:3L0I}.
HELIX 557 559 {ECO:0000244|PDB:4MXP}.
HELIX 564 579 {ECO:0000244|PDB:4MXP}.
HELIX 585 596 {ECO:0000244|PDB:4MXP}.
HELIX 599 605 {ECO:0000244|PDB:4MXP}.
HELIX 610 615 {ECO:0000244|PDB:4MXP}.
HELIX 620 645 {ECO:0000244|PDB:4MXP}.
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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