ID GTAB_STAAM Reviewed; 288 AA. AC Q99RD4; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 108. 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; OrderedLocusNames=SAV2500; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu50 / ATCC 700699; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). 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 --------------------------------------------------------------------------- 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; BA000017; BAB58662.1; -; Genomic_DNA. DR RefSeq; WP_000721336.1; NC_002758.2. DR AlphaFoldDB; Q99RD4; -. DR SMR; Q99RD4; -. DR KEGG; sav:SAV2500; -. DR HOGENOM; CLU_029499_1_2_9; -. DR PhylomeDB; Q99RD4; -. DR UniPathway; UPA00894; -. DR Proteomes; UP000002481; 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. DR World-2DPAGE; 0002:Q99RD4; -. PE 3: Inferred from homology; KW Carbohydrate metabolism; Nucleotidyltransferase; Transferase. FT CHAIN 1..288 FT /note="UTP--glucose-1-phosphate uridylyltransferase" FT /id="PRO_0000308305" 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 //