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Q05852

- GTAB_BACSU

UniProt

Q05852 - GTAB_BACSU

Protein

UTP--glucose-1-phosphate uridylyltransferase

Gene

gtaB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP. This is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since UDP-glucose serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required for biofilm formation. This is likely due to another role of UDP-glucose, which might also act as a metabolic signal regulating biofilm formation or may be involved in some unknown biosynthetic pathway essential for biofilm formation, e.g. the synthesis of an exopolysaccharide.4 Publications

    Catalytic activityi

    UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.

    Pathwayi

    GO - Molecular functioni

    1. UTP:glucose-1-phosphate uridylyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. enterobacterial common antigen biosynthetic process Source: UniProtKB-UniPathway
    2. response to stress Source: UniProtKB-KW
    3. UDP-glucose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Stress response

    Enzyme and pathway databases

    BioCyciBSUB:BSU35670-MONOMER.
    MetaCyc:MONOMER-8824.
    UniPathwayiUPA00894.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UTP--glucose-1-phosphate uridylyltransferase (EC:2.7.7.9)
    Alternative name(s):
    Alpha-D-glucosyl-1-phosphate uridylyltransferase
    General stress protein 33
    Short name:
    GSP33
    UDP-glucose pyrophosphorylase
    Short name:
    UDPGP
    Uridine diphosphoglucose pyrophosphorylase
    Gene namesi
    Name:gtaB
    Ordered Locus Names:BSU35670
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU35670. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 292292UTP--glucose-1-phosphate uridylyltransferasePRO_0000201364Add
    BLAST

    Proteomic databases

    PaxDbiQ05852.

    Expressioni

    Inductioni

    By heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation. Expressed under control of the sigma-B transcription factor.1 Publication

    Interactioni

    Protein-protein interaction databases

    IntActiQ05852. 1 interaction.
    MINTiMINT-8365569.
    STRINGi224308.BSU35670.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05852.
    SMRiQ05852. Positions 1-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UDPGP type 2 family.Curated

    Phylogenomic databases

    eggNOGiCOG1210.
    HOGENOMiHOG000283477.
    KOiK00963.
    OMAiMDEIMTN.
    OrthoDBiEOG6Z9B3V.
    PhylomeDBiQ05852.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR005771. GalU_uridylyltTrfase_bac/arc.
    IPR005835. NTP_transferase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF00483. NTP_transferase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR01099. galU. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q05852-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKVRKAIIP AAGLGTRFLP ATKAMPKEML PIVDKPTIQY IIEEAVEAGI    50
    EDIIIVTGKS KRAIEDHFDY SPELERNLEE KGKTELLEKV KKASNLADIH 100
    YIRQKEPKGL GHAVWCARNF IGDEPFAVLL GDDIVQAETP GLRQLMDEYE 150
    KTLSSIIGVQ QVPEEETHRY GIIDPLTSEG RRYQVKNFVE KPPKGTAPSN 200
    LAILGRYVFT PEIFMYLEEQ QVGAGGEIQL TDAIQKLNEI QRVFAYDFEG 250
    KRYDVGEKLG FITTTLEFAM QDKELRDQLV PFMEGLLNKE EI 292
    Length:292
    Mass (Da):33,070
    Last modified:October 1, 1994 - v1
    Checksum:iDFA640840826596F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12272 Unassigned DNA. Translation: AAA71967.1.
    Z22516 Genomic DNA. Translation: CAA80241.1.
    AL009126 Genomic DNA. Translation: CAB15584.1.
    PIRiA40650.
    RefSeqiNP_391447.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15584; CAB15584; BSU35670.
    GeneIDi936797.
    KEGGibsu:BSU35670.
    PATRICi18979144. VBIBacSub10457_3734.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12272 Unassigned DNA. Translation: AAA71967.1 .
    Z22516 Genomic DNA. Translation: CAA80241.1 .
    AL009126 Genomic DNA. Translation: CAB15584.1 .
    PIRi A40650.
    RefSeqi NP_391447.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali Q05852.
    SMRi Q05852. Positions 1-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q05852. 1 interaction.
    MINTi MINT-8365569.
    STRINGi 224308.BSU35670.

    Proteomic databases

    PaxDbi Q05852.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15584 ; CAB15584 ; BSU35670 .
    GeneIDi 936797.
    KEGGi bsu:BSU35670.
    PATRICi 18979144. VBIBacSub10457_3734.

    Organism-specific databases

    GenoListi BSU35670. [Micado ]

    Phylogenomic databases

    eggNOGi COG1210.
    HOGENOMi HOG000283477.
    KOi K00963.
    OMAi MDEIMTN.
    OrthoDBi EOG6Z9B3V.
    PhylomeDBi Q05852.

    Enzyme and pathway databases

    UniPathwayi UPA00894 .
    BioCyci BSUB:BSU35670-MONOMER.
    MetaCyc:MONOMER-8824.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR005771. GalU_uridylyltTrfase_bac/arc.
    IPR005835. NTP_transferase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    Pfami PF00483. NTP_transferase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    TIGRFAMsi TIGR01099. galU. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Bacillus subtilis gtaB encodes UDP-glucose pyrophosphorylase and is controlled by stationary-phase transcription factor sigma B."
      Varon D., Boylan S.A., Okamoto K., Price C.W.
      J. Bacteriol. 175:3964-3971(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, ROLE IN GLYCOSYLATION OF WTAS.
      Strain: 168.
    2. "Sequencing and analysis of the divergon comprising gtaB, the structural gene of UDP-glucose pyrophosphorylase of Bacillus subtilis 168."
      Soldo B., Lazarevic V., Margot P., Karamata D.
      J. Gen. Microbiol. 139:3185-3195(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: 168.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
      Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
      Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-21.
      Strain: 168 / IS58.
    5. "The gtaB marker in Bacillus subtilis 168 is associated with a deficiency in UDPglucose pyrophosphorylase."
      Pooley H.M., Paschoud D., Karamata D.
      J. Gen. Microbiol. 133:3481-3493(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 168.
    6. "Bacillus subtilis alpha-phosphoglucomutase is required for normal cell morphology and biofilm formation."
      Lazarevic V., Soldo B., Medico N., Pooley H.M., Bron S., Karamata D.
      Appl. Environ. Microbiol. 71:39-45(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN BIOFILM FORMATION, PATHWAY.
      Strain: 168.

    Entry informationi

    Entry nameiGTAB_BACSU
    AccessioniPrimary (citable) accession number: Q05852
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3