GALU_SHIFL
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 25-MAY-2022, entry version 104.
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; Proteobacteria; 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}.
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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 EnsemblBacteria; AAN42849; AAN42849; SF1236.
DR EnsemblBacteria; AAP16734; AAP16734; S1322.
DR GeneID; 1024213; -.
DR GeneID; 66674942; -.
DR KEGG; sfl:SF1236; -.
DR KEGG; sfx:S1322; -.
DR PATRIC; fig|198214.7.peg.1454; -.
DR HOGENOM; CLU_029499_1_1_6; -.
DR OMA; KRYDVGN; -.
DR OrthoDB; 1402673at2; -.
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 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 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
