ID   GTAB_STAHJ              Reviewed;         288 AA.
AC   Q4L8Y7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=SH0579;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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}.
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DR   EMBL; AP006716; BAE03888.1; -; Genomic_DNA.
DR   RefSeq; WP_011274904.1; NC_007168.1.
DR   AlphaFoldDB; Q4L8Y7; -.
DR   SMR; Q4L8Y7; -.
DR   STRING; 279808.SH0579; -.
DR   EnsemblBacteria; BAE03888; BAE03888; SH0579.
DR   GeneID; 58063229; -.
DR   KEGG; sha:SH0579; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_2_9; -.
DR   OMA; MKYITSV; -.
DR   OrthoDB; 1402673at2; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000000543; 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_0000308312"
SQ   SEQUENCE   288 AA;  32677 MW;  235203728F3AFB92 CRC64;
     MKQIKKAIIP AAGLGTRFLP ATKAMPKEML PILDKPTIQY IVEEASRAGI EDIIIVTGKH
     KRAIEDHFDN QKELEMVLEE KGKDDLLEKV QYSTDLANIF YVRQKEQKGL GHAIHTARQF
     IGNEPFAVLL GDDIVESETP AIKQLMNVYE ETGHSVIGVQ EVPESVTHRY GIIDPLEKEG
     RRYEVKQFVE KPKQGTAPSN LAIMGRYILT PEIFDYLETQ KEGAGNEIQL TDAIERMNSD
     IPVYAYDFDG DRYDVGEKLG FVKTTIEYAL KDPKMKDELI KFIKELGF