ID GTAB2_STAS1 Reviewed; 289 AA. AC Q49VP4; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase 2; DE EC=2.7.7.9; DE AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase 2; DE AltName: Full=UDP-glucose pyrophosphorylase 2; DE Short=UDPGP 2; DE AltName: Full=Uridine diphosphoglucose pyrophosphorylase 2; GN Name=gtaB2; OrderedLocusNames=SSP2021; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM OS 20229 / NCIMB 8711 / NCTC 7292 / S-41). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=342451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41; RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.; RT "Whole genome sequence of Staphylococcus saprophyticus reveals the RT pathogenesis of uncomplicated urinary tract infection."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005). 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. a glycolipid found in the CC membrane, which is also used as a membrane anchor for lipoteichoic acid CC (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; AP008934; BAE19166.1; -; Genomic_DNA. DR RefSeq; WP_011303674.1; NZ_MTGA01000039.1. DR AlphaFoldDB; Q49VP4; -. DR SMR; Q49VP4; -. DR GeneID; 66868180; -. DR KEGG; ssp:SSP2021; -. DR eggNOG; COG1210; Bacteria. DR HOGENOM; CLU_029499_1_2_9; -. DR OrthoDB; 9803871at2; -. DR UniPathway; UPA00894; -. DR Proteomes; UP000006371; 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; Reference proteome; KW Transferase. FT CHAIN 1..289 FT /note="UTP--glucose-1-phosphate uridylyltransferase 2" FT /id="PRO_0000308314" SQ SEQUENCE 289 AA; 32658 MW; D8140ABBCCAEB036 CRC64; MRKIKKAIIP AAGLGTRFLP ATKAMPKEML PILDKPTIQY IVEEAARAGI EDIIIVTGKH KRAIEDHFDN QKELEMILQE KGKTDLLEKV KYSTELANIF YVRQKEQKGL GHAIYSARQF IGDEPFAVLL GDDIVESDNP AIKQLIEAYE ETGKSVIGVQ EVDEAQTHRY GIIDPLQKFG RKYEVNEFVE KPKQGTAPSN LAIMGRYVLT PDIFDYLATQ GEGAGGEIQL TDAIERLNRA DQVYAYDFEG DRYDVGEKLG FVKTTIEYAL KDESMHDELV EFIKKLKLN //