ID   GTAB_BACSU              Reviewed;         292 AA.
AC   Q05852;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE            EC=2.7.7.9;
DE   AltName: Full=UDP-glucose pyrophosphorylase;
DE            Short=UDPGP;
DE   AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase;
DE   AltName: Full=Uridine diphosphoglucose pyrophosphorylase;
DE   AltName: Full=General stress protein 33;
DE            Short=GSP33;
GN   Name=gtaB; OrderedLocusNames=BSU35670;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND ROLE IN
RP   GLYCOSYLATION OF WTAS.
RC   STRAIN=168;
RX   MEDLINE=93308074; PubMed=8320212;
RA   Varon D., Boylan S.A., Okamoto K., Price C.W.;
RT   "Bacillus subtilis gtaB encodes UDP-glucose pyrophosphorylase and is
RT   controlled by stationary-phase transcription factor sigma B.";
RL   J. Bacteriol. 175:3964-3971(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=168;
RX   MEDLINE=94172311; PubMed=8126437;
RA   Soldo B., Lazarevic V., Margot P., Karamata D.;
RT   "Sequencing and analysis of the divergon comprising gtaB, the
RT   structural gene of UDP-glucose pyrophosphorylase of Bacillus subtilis
RT   168.";
RL   J. Gen. Microbiol. 139:3185-3195(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-21.
RC   STRAIN=168 / IS58;
RX   MEDLINE=97443988; PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [5]
RP   FUNCTION.
RC   STRAIN=168;
RX   PubMed=2846750;
RA   Pooley H.M., Paschoud D., Karamata D.;
RT   "The gtaB marker in Bacillus subtilis 168 is associated with a
RT   deficiency in UDPglucose pyrophosphorylase.";
RL   J. Gen. Microbiol. 133:3481-3493(1987).
RN   [6]
RP   ROLE IN BIOFILM FORMATION, AND PATHWAY.
RC   STRAIN=168;
RX   PubMed=15640167; DOI=10.1128/AEM.71.1.39-45.2005;
RA   Lazarevic V., Soldo B., Medico N., Pooley H.M., Bron S., Karamata D.;
RT   "Bacillus subtilis alpha-phosphoglucomutase is required for normal
RT   cell morphology and biofilm formation.";
RL   Appl. Environ. Microbiol. 71:39-45(2005).
CC   -!- FUNCTION: Catalyzes the formation of UDP-glucose from glucose-1-
CC       phosphate and UTP. This is an intermediate step in the
CC       biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the
CC       predominant glycolipid found in B.subtilis membrane, which is also
CC       used as a membrane anchor for lipoteichoic acid (LTA). Has a role
CC       in the biosynthesis of all phosphate-containing envelope polymers,
CC       since UDP-glucose serves as a glucosyl donor not only for the
CC       biosynthesis of LTA but also for wall teichoic acids (WTAs). Is
CC       required for biofilm formation. This is likely due to another role
CC       of UDP-glucose, which might also act as a metabolic signal
CC       regulating biofilm formation or may be involved in some unknown
CC       biosynthetic pathway essential for biofilm formation, e.g. the
CC       synthesis of an exopolysaccharide.
CC   -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate =
CC       diphosphate + UDP-glucose.
CC   -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol
CC       biosynthesis.
CC   -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC       limitation and oxygen limitation. Expressed under control of the
CC       sigma-B transcription factor.
CC   -!- SIMILARITY: Belongs to the UDPGP type 2 family.
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DR   EMBL; L12272; AAA71967.1; -; Unassigned_DNA.
DR   EMBL; Z22516; CAA80241.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15584.1; -; Genomic_DNA.
DR   PIR; A40650; A40650.
DR   RefSeq; NP_391447.1; -.
DR   HSSP; Q9F7K6; 1IIN.
DR   GeneID; 936797; -.
DR   GenomeReviews; AL009126_GR; BSU35670.
DR   KEGG; bsu:BSU35670; -.
DR   NMPDR; fig|224308.1.peg.3573; -.
DR   SubtiList; BG10402; gtaB.
DR   HOGENOM; Q05852; -.
DR   OMA; Q05852; MVATMEV.
DR   BioCyc; BSUB224308:BSU3564-MON; -.
DR   BioCyc; MetaCyc:MON-8824; -.
DR   BRENDA; 2.7.7.9; 150.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase...; IEA:EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   InterPro; IPR005771; GalU_trans_bac.
DR   InterPro; IPR005835; NTP_transferase.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   TIGRFAMs; TIGR01099; galU; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW   Nucleotidyltransferase; Stress response; Transferase.
FT   CHAIN         1    292       UTP--glucose-1-phosphate
FT                                uridylyltransferase.
FT                                /FTId=PRO_0000201364.
SQ   SEQUENCE   292 AA;  33070 MW;  DFA640840826596F CRC64;
     MKKVRKAIIP AAGLGTRFLP ATKAMPKEML PIVDKPTIQY IIEEAVEAGI EDIIIVTGKS
     KRAIEDHFDY SPELERNLEE KGKTELLEKV KKASNLADIH YIRQKEPKGL GHAVWCARNF
     IGDEPFAVLL GDDIVQAETP GLRQLMDEYE KTLSSIIGVQ QVPEEETHRY GIIDPLTSEG
     RRYQVKNFVE KPPKGTAPSN LAILGRYVFT PEIFMYLEEQ QVGAGGEIQL TDAIQKLNEI
     QRVFAYDFEG KRYDVGEKLG FITTTLEFAM QDKELRDQLV PFMEGLLNKE EI
//