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   03-AUG-2022, entry version 102.
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; Firmicutes; 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}.
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DR   EMBL; BA000017; BAB58662.1; -; Genomic_DNA.
DR   RefSeq; WP_000721336.1; NC_002758.2.
DR   AlphaFoldDB; Q99RD4; -.
DR   SMR; Q99RD4; -.
DR   World-2DPAGE; 0002:Q99RD4; -.
DR   PaxDb; Q99RD4; -.
DR   EnsemblBacteria; BAB58662; BAB58662; SAV2500.
DR   KEGG; sav:SAV2500; -.
DR   HOGENOM; CLU_029499_1_2_9; -.
DR   OMA; MHYVRQG; -.
DR   PhylomeDB; Q99RD4; -.
DR   BioCyc; SAUR158878:SAV_RS13635-MON; -.
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   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43197; PTHR43197; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01099; galU; 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_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