Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Multifunctional virulence effector protein DrrA

Gene

drrA

Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Status
Reviewed-Annotation score: -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]-L-tyrosine = diphosphate + [protein]-O4-(5'-adenylyl)-L-tyrosine.
ATP + [protein]-L-threonine = diphosphate + [protein]-O4-(5'-adenylyl)-L-threonine.
GTP + [protein]-L-tyrosine = diphosphate + [protein]-O4-(5'-guanylyl)-L-tyrosine.

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

Keywordsi

Molecular functionGuanine-nucleotide releasing factor, Multifunctional enzyme, Nucleotidyltransferase, Transferase
Biological processVirulence
LigandATP-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

GO - Cellular componenti

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
PRIDEiQ5ZSQ3

Interactioni

Subunit structurei

Interacts with host RAB1A.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAB1AP628207EBI-7632432,EBI-716845From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ5ZSQ3, 1 interactor
MINTiQ5ZSQ3
STRINGi272624.lpg2464

Structurei

Secondary structure

1647
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiAQATEYS

Family and domain databases

CDDicd11689 SidM_DrrA_GEF, 1 hit
Gene3Di1.20.1280.280, 1 hit
InterProiView protein in InterPro
IPR033784 DrrA_GEF
IPR028057 DrrA_P4M
IPR038346 DrrA_PI4P-bd_sf
PfamiView protein in Pfam
PF14860 DrrA_P4M, 1 hit

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
PATRICifig|272624.6.peg.2613

Similar proteinsi

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
MINTiQ5ZSQ3
STRINGi272624.lpg2464

Proteomic databases

PaxDbiQ5ZSQ3
PRIDEiQ5ZSQ3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU28524; AAU28524; lpg2464
GeneIDi19834029
KEGGilpn:lpg2464
PATRICifig|272624.6.peg.2613

Phylogenomic databases

HOGENOMiHOG000126893
KOiK15480
OMAiAQATEYS

Miscellaneous databases

EvolutionaryTraceiQ5ZSQ3

Family and domain databases

CDDicd11689 SidM_DrrA_GEF, 1 hit
Gene3Di1.20.1280.280, 1 hit
InterProiView protein in InterPro
IPR033784 DrrA_GEF
IPR028057 DrrA_P4M
IPR038346 DrrA_PI4P-bd_sf
PfamiView protein in Pfam
PF14860 DrrA_P4M, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDRRA_LEGPH
AccessioniPrimary (citable) accession number: Q5ZSQ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: November 23, 2004
Last modified: May 23, 2018
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again