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   25-MAY-2022, entry version 72.
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; Firmicutes; 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};
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DR   EMBL; CP000255; ABD22300.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000721336.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FE05; -.
DR   SMR; Q2FE05; -.
DR   EnsemblBacteria; ABD22300; ABD22300; SAUSA300_2439.
DR   KEGG; saa:SAUSA300_2439; -.
DR   HOGENOM; CLU_029499_1_3_9; -.
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   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_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