YNGB_BACSU
ID YNGB_BACSU Reviewed; 297 AA.
AC O31822;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase YngB {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=UDP-glucose pyrophosphorylase;
DE Short=UDPGP;
DE Short=UGPase {ECO:0000303|PubMed:33556370};
DE AltName: Full=Uridine diphosphoglucose pyrophosphorylase;
DE Flags: Precursor;
GN Name=yngB; OrderedLocusNames=BSU18180;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2] {ECO:0007744|PDB:7B1R}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-297, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
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).
RN [3] {ECO:0007744|PDB:7O2N}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-297.
RA Wu C.;
RT "Structural and functional characterisation of the Bacillus subtilis
RT uridylyltransferase YngB.";
RL Submitted (MAR-2021) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the formation of UDP-glucose from glucose-1-
CC phosphate and UTP (PubMed:33556370). This is an intermediate step in
CC the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the
CC predominant glycolipid found in B.subtilis membrane, which is also used
CC as a membrane anchor for lipoteichoic acid (LTA) (PubMed:33556370).
CC YngB contributes to wall teichoic acid (WTA) glucosylation and
CC glycolipid formation under anaerobic fermentative growth conditions
CC (PubMed:33556370). Might also enter other glycosylation pathways,
CC leading to the decorating of other cell envelope components with
CC glucose residues under anaerobic or other growth conditions
CC (PubMed:33556370). {ECO:0000269|PubMed:33556370}.
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=42.1 uM for glucose-1-phosphate {ECO:0000269|PubMed:33556370};
CC KM=62.9 uM for UTP {ECO:0000269|PubMed:33556370};
CC Note=kcat is 0.264 sec(-1) with glucose-1-phosphate as substrate.
CC kcat is 0.293 sec(-1) with UTP as substrate.
CC {ECO:0000269|PubMed:33556370};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000305|PubMed:33556370}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:33556370}.
CC -!- INDUCTION: Expressed under anaerobic conditions.
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}.
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DR EMBL; AL009126; CAB13701.1; -; Genomic_DNA.
DR PIR; G69892; G69892.
DR RefSeq; NP_389700.1; NC_000964.3.
DR RefSeq; WP_003245127.1; NZ_JNCM01000035.1.
DR PDB; 7B1R; X-ray; 2.80 A; A/B=2-297.
DR PDB; 7O2N; X-ray; 2.80 A; A/B=2-297.
DR PDBsum; 7B1R; -.
DR PDBsum; 7O2N; -.
DR AlphaFoldDB; O31822; -.
DR SMR; O31822; -.
DR STRING; 224308.BSU18180; -.
DR PaxDb; O31822; -.
DR PRIDE; O31822; -.
DR EnsemblBacteria; CAB13701; CAB13701; BSU_18180.
DR GeneID; 936791; -.
DR KEGG; bsu:BSU18180; -.
DR PATRIC; fig|224308.179.peg.1983; -.
DR eggNOG; COG1210; Bacteria.
DR InParanoid; O31822; -.
DR OMA; LCAEHFI; -.
DR PhylomeDB; O31822; -.
DR BioCyc; BSUB:BSU18180-MON; -.
DR UniPathway; UPA00894; -.
DR Proteomes; UP000001570; Chromosome.
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 3D-structure; Carbohydrate metabolism; Nucleotidyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..297
FT /note="UTP--glucose-1-phosphate uridylyltransferase YngB"
FT /id="PRO_0000389480"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:7B1R"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:7B1R"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 201..211
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:7B1R"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:7B1R"
FT HELIX 274..296
FT /evidence="ECO:0007829|PDB:7B1R"
SQ SEQUENCE 297 AA; 33147 MW; 535EEA3A567E7C97 CRC64;
MRKKVRKAVI PAAGLGTRFL PATKAQPKEM LPIVDKPAIQ YIVEEAAESG IEDILIITGR
NKRSIEDHFD RSAELEFNLR EKGKTETLKE MQQIADLANI HYIRQKEPLG LGHAVLCAEH
FIGDEPFAVL LGDDIMVSET PALRQLMDVY DVYGTEVVGV QSVLPEDVSK YGIINTSGSQ
GHVYEVNDLV EKPSPEEAPS EIAVMGRYVL NSSIFSVLKT IGRGAGNEIQ LTDALREVCR
KEPIHARLLE GNRYDIGDKL GCFKASTEIG LMRPEMRSQL LAYLEDVIKR ETKEMLR
