ID   GALU_SHIFL              Reviewed;         302 AA.
AC   P0AEP6; P25520;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 112.
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=galU; OrderedLocusNames=SF1236, S1322;
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION OF ROLE IN LPS
RP   SYNTHESIS AND VIRULENCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=7528731; DOI=10.1128/iai.63.1.229-237.1995;
RA   Sandlin R.C., Lampel K.A., Keasler S.P., Goldberg M.B., Stolzer A.L.,
RA   Maurelli A.T.;
RT   "Avirulence of rough mutants of Shigella flexneri: requirement of O antigen
RT   for correct unipolar localization of IcsA in the bacterial outer
RT   membrane.";
RL   Infect. Immun. 63:229-237(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: May play a role in stationary phase survival. {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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- SUBUNIT: Homotetramer or homopentamer. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: A transposon mutant in galU (only the first 220
CC       residues could be expressed) allows HeLa cell invasion but no cell
CC       spreading. Shows decreased secretion of IscA, a protein required for
CC       cell spreading. The lipopolysaccharide produced is of a size consistent
CC       with it containing only lipid A and a single core component.
CC       {ECO:0000269|PubMed:7528731}.
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; L32811; AAD15244.1; -; Genomic_DNA.
DR   EMBL; AE005674; AAN42849.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16734.1; -; Genomic_DNA.
DR   RefSeq; NP_707142.1; NC_004337.2.
DR   RefSeq; WP_000718995.1; NZ_WPGW01000029.1.
DR   AlphaFoldDB; P0AEP6; -.
DR   SMR; P0AEP6; -.
DR   STRING; 198214.SF1236; -.
DR   PaxDb; 198214-SF1236; -.
DR   GeneID; 1024213; -.
DR   GeneID; 75203349; -.
DR   KEGG; sfl:SF1236; -.
DR   KEGG; sfx:S1322; -.
DR   PATRIC; fig|198214.7.peg.1454; -.
DR   HOGENOM; CLU_029499_1_1_6; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009103; P:lipopolysaccharide 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   1: Evidence at protein level;
KW   Lipopolysaccharide biosynthesis; Magnesium; Nucleotidyltransferase;
KW   Reference proteome; Transferase; Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..302
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000201363"
SQ   SEQUENCE   302 AA;  32942 MW;  ADEAEB3F6A1194CB CRC64;
     MAAINTKVKK AVIPVAGLGT RMLPATKAIP KEMLPLVDKP LIQYVVNECI AAGITEIVLV
     THSSKNSIEN HFDTSFELEA MLEKRVKRQL LDEVQSICPP HVTIMQVRQG LAKGLGHAVL
     CAHPVVGDEP VAVILPDVIL DEYESDLSQD NLAEMIRRFD ETGHSQIMVE PVADVTAYGV
     VDCKGVELAP GESVPMVGVV EKPKADVAPS NLAIVGRYVL SADIWPLLAK TPPGAGDEIQ
     LTDAIDMLIE KETVEAYHMK GKSHDCGNKL GYMQAFVEYG IRHNTLGTEF KAWLEEEMGI
     KK
//