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Q99RD4 (GTAB_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
UTP--glucose-1-phosphate uridylyltransferase

EC=2.7.7.9
Alternative name(s):
Alpha-D-glucosyl-1-phosphate uridylyltransferase
UDP-glucose pyrophosphorylase
Short name=UDPGP
Uridine diphosphoglucose pyrophosphorylase
Gene names
Name:gtaB
Ordered Locus Names:SAV2500
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP. This is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in the S.aureus membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA) By similarity.

Catalytic activity

UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.

Pathway

Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.

Sequence similarities

Belongs to the UDPGP type 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288UTP--glucose-1-phosphate uridylyltransferase
PRO_0000308305

Sequences

Sequence LengthMass (Da)Tools
Q99RD4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 126BF005599D4418

FASTA28832,451
        10         20         30         40         50         60 
MKKIKKAIIP AAGLGTRFLP ATKAMPKEML PILDKPTIQY IVEEAARAGI EDIIIVTGRH 

        70         80         90        100        110        120 
KRAIEDHFDS QKELEMVLKE KGKSELLEKV QYSTELANIF YVRQKEQKGL GHAISSARQF 

       130        140        150        160        170        180 
IGNEPFAVLL GDDIVESEVP AVKQLIDVYE ETGHSVIGVQ EVPEADTHRY GIIDPLTKNG 

       190        200        210        220        230        240 
RQYEVKKFVE KPAQGTAPSN LAIMGRYVLT PEIFDYLKTQ KEGAGNEIQL TDAIERMNND 

       250        260        270        280 
NQVYAYDFEG ERYDVGEKLG FVKTTIEYAL KDDSMREELT RFIKALGL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB58662.1.
RefSeqNP_373024.1. NC_002758.2.

3D structure databases

ProteinModelPortalQ99RD4.
SMRQ99RD4. Positions 1-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158878.SAV2500.

2D gel databases

World-2DPAGE0002:Q99RD4.

Proteomic databases

PRIDEQ99RD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB58662; BAB58662; SAV2500.
GeneID1122525.
KEGGsav:SAV2500.
PATRIC19565928. VBIStaAur52173_2590.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1210.
HOGENOMHOG000283477.
KOK00963.
OMAKLIDECS.
OrthoDBEOG6Z9B3V.
PhylomeDBQ99RD4.

Enzyme and pathway databases

BioCycSAUR158878:GJJ5-2568-MONOMER.
UniPathwayUPA00894.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR005771. GalU_uridylyltTrfase_bac/arc.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
TIGRFAMsTIGR01099. galU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGTAB_STAAM
AccessionPrimary (citable) accession number: Q99RD4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways