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Protein

Multifunctional virulence effector protein DrrA

Gene

drrA

Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (PtdIns4P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection.6 Publications

Catalytic activityi

ATP + [protein] = diphosphate + [protein]-AMP.
GTP + [protein] = diphosphate + [protein]-GMP.

GO - Molecular functioni

GO - Biological processi

  • pathogenesis Source: UniProtKB
  • protein adenylylation Source: UniProtKB
  • protein guanylylation Source: UniProtKB
  • protein targeting to membrane Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Virulence

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Multifunctional virulence effector protein DrrA
Alternative name(s):
Defects in Rab1 recruitment protein A
Including the following 2 domains:
Adenosine monophosphate-protein transferase (EC:2.7.7.n1)
Short name:
AMPylator
Alternative name(s):
Guanosine monophosphate-protein transferase (EC:2.7.7.n6)
Short name:
GMPylator
Rab1 guanine nucleotide exchange factor
Gene namesi
Name:drrA
Synonyms:sidM
Ordered Locus Names:lpg2464
OrganismiLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Taxonomic identifieri272624 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
Proteomesi
  • UP000000609 Componenti: Chromosome

Subcellular locationi

  • Secreted 1 Publication
  • Host cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication

  • Note: Translocated into the host cell via the type IV secretion system (T4SS). Membrane association is mediated by PtdIns4P-binding.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasmic vesicle, Host membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi410W → D: Almost abolishes GEF and GDF activities, but still binds Rab1. 1 Publication1
Mutagenesisi431G → D: Abolishes GEF and GDF activities, but still binds Rab1. 1 Publication1
Mutagenesisi435A → D or E: Abolishes GEF and GDF activities, but still binds Rab1. 2 Publications1
Mutagenesisi451 – 453NER → AEA: Almost abolishes GEF and GDF activities, with a more severe effect on GEF activity. 2 Publications3
Mutagenesisi480D → A: Slightly impairs GEF and GDF activities; when associated with A-483. 1 Publication1
Mutagenesisi483S → A: Slightly impairs GEF and GDF activities; when associated with A-480. 1 Publication1
Mutagenesisi541R → A: Abolishes PtdIns(4)P-binding; when associated with A-568. 1 Publication1
Mutagenesisi568K → A: Abolishes PtdIns(4)P-binding; when associated with A-541 or A-619. 1 Publication1
Mutagenesisi619T → A: Abolishes PtdIns(4)P-binding; when associated with A-568. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004175451 – 647Multifunctional virulence effector protein DrrAAdd BLAST647

Proteomic databases

PaxDbiQ5ZSQ3.

Interactioni

Subunit structurei

Interacts with host RAB1A.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAB1AP628207EBI-7632432,EBI-716845From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ5ZSQ3. 1 interactor.
MINTiMINT-7720716.

Structurei

Secondary structure

1647
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi214 – 224Combined sources11
Helixi240 – 243Combined sources4
Helixi245 – 258Combined sources14
Helixi271 – 280Combined sources10
Helixi286 – 307Combined sources22
Helixi320 – 322Combined sources3
Helixi336 – 361Combined sources26
Helixi365 – 381Combined sources17
Helixi386 – 389Combined sources4
Helixi390 – 393Combined sources4
Helixi400 – 419Combined sources20
Helixi428 – 447Combined sources20
Beta strandi450 – 452Combined sources3
Helixi458 – 460Combined sources3
Helixi464 – 478Combined sources15
Helixi490 – 506Combined sources17
Helixi512 – 520Combined sources9
Beta strandi526 – 528Combined sources3
Turni530 – 533Combined sources4
Helixi557 – 559Combined sources3
Helixi564 – 579Combined sources16
Helixi585 – 596Combined sources12
Helixi599 – 605Combined sources7
Helixi610 – 615Combined sources6
Helixi620 – 645Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WWXX-ray1.50B317-533[»]
3JZ9X-ray1.80A340-533[»]
3JZAX-ray1.80B340-533[»]
3L0IX-ray2.85A/C193-550[»]
3L0MX-ray3.45A/B317-647[»]
3N6OX-ray2.50A/B340-647[»]
4MXPX-ray1.83A330-647[»]
SMRiQ5ZSQ3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5ZSQ3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 339Adenosine monophosphate-protein transferaseAdd BLAST339
Regioni340 – 520Rab1 guanine nucleotide exchange factorAdd BLAST181
Regioni544 – 647P4M regionAdd BLAST104

Domaini

The P4M (PtdIns4P-binding) region mediates binding to PtdIns4P and membrane attachment.By similarity

Sequence similaritiesi

Belongs to the DrrA family.Curated

Phylogenomic databases

HOGENOMiHOG000126893.
KOiK15480.
OMAiIRENEGN.

Family and domain databases

CDDicd11689. SidM_DrrA_GEF. 1 hit.
InterProiIPR033784. DrrA_GEF.
IPR028057. DrrA_P4M.
[Graphical view]
PfamiPF14860. DrrA_P4M. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5ZSQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIMGRIKMS VNEEQFGSLY SDERDKPLLS PTAQKKFEEY QNKLANLSKI
60 70 80 90 100
IRENEGNEVS PWQEWENGLR QIYKEMIYDA FDALGVEMPK DMEVHFAGSL
110 120 130 140 150
AKAQATEYSD LDAFVIVKND EDIKKVKPVF DALNNLCQRI FTASNQIYPD
160 170 180 190 200
PIGINPSRLI GTPDDLFGML KDGMVADVEA TAMSILTSKP VLPRYELGEE
210 220 230 240 250
LRDKIKQEPS FSNMVSAKKF YNKAIKDFTA PKEGAEVVSV KTHIMRPIDF
260 270 280 290 300
MLMGLREEFN LYSEDGAHLS APGTIRLLRE KNLLPEEQIA RIESVYNQAM
310 320 330 340 350
SKRFELHAEH KKEHDEMPYS DAKAMLDEVA KIRELGVQRV TRIENLENAK
360 370 380 390 400
KLWDNANSML EKGNISGYLK AANELHKFMK EKNLKEDDLR PELSDKTISP
410 420 430 440 450
KGYAILQSLW GAASDYSRAA ATLTESTVEP GLVSAVNKMS AFFMDCKLSP
460 470 480 490 500
NERATPDPDF KVGKSKILVG IMQFIKDVAD PTSKIWMHNT KALMNHKIAA
510 520 530 540 550
IQKLERSNNV NDETLESVLS SKGENLSEYL SYKYATKDEG REHRYTASTE
560 570 580 590 600
NFKNVKEKYQ QMRGDALKTE ILADFKDKLA EATDEQSLKQ IVAELKSKDE
610 620 630 640
YRILAKGQGL TTQLLGLKTS SVSSFEKMVE ETRESIKSQE RQTIKIK
Length:647
Mass (Da):73,422
Last modified:November 23, 2004 - v1
Checksum:iDCE6EC98BCC3CDCA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ845395 mRNA. Translation: ABG90503.1.
AE017354 Genomic DNA. Translation: AAU28524.1.
RefSeqiWP_010948166.1. NC_002942.5.
YP_096471.1. NC_002942.5.

Genome annotation databases

EnsemblBacteriaiAAU28524; AAU28524; lpg2464.
GeneIDi19834029.
KEGGilpn:lpg2464.
PATRICi22332221. VBILegPne29832_2613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ845395 mRNA. Translation: ABG90503.1.
AE017354 Genomic DNA. Translation: AAU28524.1.
RefSeqiWP_010948166.1. NC_002942.5.
YP_096471.1. NC_002942.5.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WWXX-ray1.50B317-533[»]
3JZ9X-ray1.80A340-533[»]
3JZAX-ray1.80B340-533[»]
3L0IX-ray2.85A/C193-550[»]
3L0MX-ray3.45A/B317-647[»]
3N6OX-ray2.50A/B340-647[»]
4MXPX-ray1.83A330-647[»]
SMRiQ5ZSQ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5ZSQ3. 1 interactor.
MINTiMINT-7720716.

Proteomic databases

PaxDbiQ5ZSQ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU28524; AAU28524; lpg2464.
GeneIDi19834029.
KEGGilpn:lpg2464.
PATRICi22332221. VBILegPne29832_2613.

Phylogenomic databases

HOGENOMiHOG000126893.
KOiK15480.
OMAiIRENEGN.

Miscellaneous databases

EvolutionaryTraceiQ5ZSQ3.

Family and domain databases

CDDicd11689. SidM_DrrA_GEF. 1 hit.
InterProiIPR033784. DrrA_GEF.
IPR028057. DrrA_P4M.
[Graphical view]
PfamiPF14860. DrrA_P4M. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDRRA_LEGPH
AccessioniPrimary (citable) accession number: Q5ZSQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: November 23, 2004
Last modified: November 30, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.