GTAB_BACSU
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 03-AUG-2022, entry version 130.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000303|PubMed:33556370};
DE EC=2.7.7.9 {ECO:0000269|PubMed:33556370};
DE AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase;
DE AltName: Full=General stress protein 33;
DE Short=GSP33;
DE AltName: Full=UDP-glucose pyrophosphorylase;
DE Short=UDPGP;
DE Short=UGPase {ECO:0000303|PubMed:33556370};
DE AltName: Full=Uridine diphosphoglucose pyrophosphorylase;
GN Name=gtaB; OrderedLocusNames=BSU35670;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND ROLE IN GLYCOSYLATION OF
RP WTAS.
RC STRAIN=168;
RX PubMed=8320212; DOI=10.1128/jb.175.13.3964-3971.1993;
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 PubMed=8126437; DOI=10.1099/00221287-139-12-3185;
RA Soldo B., Lazarevic V., Margot P., Karamata D.;
RT "Sequencing and analysis of the divergon comprising gtaB, the structural
RT gene of UDP-glucose pyrophosphorylase of Bacillus subtilis 168.";
RL J. Gen. Microbiol. 139:3185-3195(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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 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; DOI=10.1099/00221287-133-12-3481;
RA Pooley H.M., Paschoud D., Karamata D.;
RT "The gtaB marker in Bacillus subtilis 168 is associated with a deficiency
RT 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 cell
RT morphology and biofilm formation.";
RL Appl. Environ. Microbiol. 71:39-45(2005).
RN [7]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
RN [8]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=33556370; DOI=10.1016/j.jbc.2021.100384;
RA Wu C.H., Rismondo J., Morgan R.M.L., Shen Y., Loessner M.J.,
RA Larrouy-Maumus G., Freemont P.S., Gruendling A.;
RT "Bacillus subtilis YngB contributes to wall teichoic acid glucosylation and
RT glycolipid formation during anaerobic growth.";
RL J. Biol. Chem. 296:100384-100384(2021).
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. the predominant glycolipid
CC found in B.subtilis membrane, which is also used as a membrane anchor
CC for lipoteichoic acid (LTA). Has a role in the biosynthesis of all
CC phosphate-containing envelope polymers, since UDP-glucose serves as a
CC glucosyl donor not only for the biosynthesis of LTA but also for wall
CC teichoic acids (WTAs). Is required for biofilm formation. This is
CC likely due to another role of UDP-glucose, which might also act as a
CC metabolic signal regulating biofilm formation or may be involved in
CC some unknown biosynthetic pathway essential for biofilm formation, e.g.
CC the synthesis of an exopolysaccharide. {ECO:0000269|PubMed:15640167,
CC ECO:0000269|PubMed:2846750, ECO:0000269|PubMed:8126437,
CC ECO:0000269|PubMed:8320212}.
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 Evidence={ECO:0000269|PubMed:33556370};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45.6 uM for glucose-1-phosphate {ECO:0000269|PubMed:33556370};
CC KM=49.5 uM for UTP {ECO:0000269|PubMed:33556370};
CC Note=kcat is 1.06 sec(-1) with glucose-1-phosphate as substrate. kcat
CC is 1.04 sec(-1) with UTP as substrate. {ECO:0000269|PubMed:33556370};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000269|PubMed:15640167}.
CC -!- SUBUNIT: Interacts with FloT. {ECO:0000269|PubMed:23651456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456};
CC Peripheral membrane protein {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Peripheral membrane protein.
CC Note=Present in detergent-resistant membrane (DRM) fractions that may
CC be equivalent to eukaryotic membrane rafts; these rafts include
CC proteins involved in signaling, molecule trafficking and protein
CC secretion. {ECO:0000269|PubMed:23651456}.
CC -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC limitation and oxygen limitation. Expressed under control of the sigma-
CC B transcription factor. {ECO:0000269|PubMed:8320212}.
CC -!- DISRUPTION PHENOTYPE: Under aerobic growth condition, deletion mutants
CC display morphological defects and the cells are curled and show some
CC bulges (PubMed:33556370). No aberrant morphology is observed for the
CC deletion mutants under anaerobic growth conditions (PubMed:33556370).
CC {ECO:0000269|PubMed:33556370}.
CC -!- MISCELLANEOUS: GtaB is the main UGPase enzyme producing UDP-glucose
CC under both aerobic and anaerobic fermentative growth conditions
CC (PubMed:33556370). YngB augments UDP-glucose production under anaerobic
CC growth conditions (PubMed:33556370). {ECO:0000269|PubMed:33556370}.
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; 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; NC_000964.3.
DR RefSeq; WP_003227944.1; NZ_CP053102.1.
DR AlphaFoldDB; Q05852; -.
DR SMR; Q05852; -.
DR IntAct; Q05852; 1.
DR MINT; Q05852; -.
DR STRING; 224308.BSU35670; -.
DR jPOST; Q05852; -.
DR PaxDb; Q05852; -.
DR PRIDE; Q05852; -.
DR EnsemblBacteria; CAB15584; CAB15584; BSU_35670.
DR GeneID; 936797; -.
DR KEGG; bsu:BSU35670; -.
DR PATRIC; fig|224308.179.peg.3858; -.
DR eggNOG; COG1210; Bacteria.
DR InParanoid; Q05852; -.
DR OMA; MKYITSV; -.
DR PhylomeDB; Q05852; -.
DR BioCyc; BSUB:BSU35670-MON; -.
DR BioCyc; MetaCyc:BSU35670-MON; -.
DR UniPathway; UPA00894; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Direct protein sequencing;
KW Membrane; Nucleotidyltransferase; Reference proteome; Stress response;
KW Transferase.
FT CHAIN 1..292
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="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
