ID GTAB_STAA3 Reviewed; 288 AA. AC Q2FE05; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 27-MAR-2024, entry version 78. DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase; DE EC=2.7.7.9; DE AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase; DE AltName: Full=UDP-glucose pyrophosphorylase; DE Short=UDPGP; DE AltName: Full=Uridine diphosphoglucose pyrophosphorylase; GN Name=gtaB; Synonyms=galU; OrderedLocusNames=SAUSA300_2439; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). CC -!- FUNCTION: Catalyzes the formation of UDP-glucose from glucose-1- CC phosphate and UTP. This is an intermediate step in the biosynthesis of CC diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid CC found in the S.aureus membrane, which is also used as a membrane anchor CC for lipoteichoic acid (LTA) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP- CC alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601, CC ChEBI:CHEBI:58885; EC=2.7.7.9; CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis. CC -!- SIMILARITY: Belongs to the UDPGP type 2 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABD22300.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000255; ABD22300.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_000721336.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FE05; -. DR SMR; Q2FE05; -. DR KEGG; saa:SAUSA300_2439; -. DR HOGENOM; CLU_029499_1_3_9; -. DR OMA; MHYVRQG; -. DR UniPathway; UPA00894; -. DR Proteomes; UP000001939; Chromosome. DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro. DR CDD; cd02541; UGPase_prokaryotic; 1. DR InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR NCBIfam; TIGR01099; galU; 1. DR PANTHER; PTHR43197; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1. DR PANTHER; PTHR43197:SF1; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Nucleotidyltransferase; Transferase. FT CHAIN 1..288 FT /note="UTP--glucose-1-phosphate uridylyltransferase" FT /id="PRO_0000308302" SQ SEQUENCE 288 AA; 32451 MW; 126BF005599D4418 CRC64; MKKIKKAIIP AAGLGTRFLP ATKAMPKEML PILDKPTIQY IVEEAARAGI EDIIIVTGRH KRAIEDHFDS QKELEMVLKE KGKSELLEKV QYSTELANIF YVRQKEQKGL GHAISSARQF IGNEPFAVLL GDDIVESEVP AVKQLIDVYE ETGHSVIGVQ EVPEADTHRY GIIDPLTKNG RQYEVKKFVE KPAQGTAPSN LAIMGRYVLT PEIFDYLKTQ KEGAGNEIQL TDAIERMNND NQVYAYDFEG ERYDVGEKLG FVKTTIEYAL KDDSMREELT RFIKALGL //