TAGE_BACSU
ID TAGE_BACSU Reviewed; 673 AA.
AC P13484;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Poly(glycerol-phosphate) alpha-glucosyltransferase;
DE EC=2.4.1.52 {ECO:0000269|PubMed:21558268};
DE AltName: Full=Major teichoic acid biosynthesis protein E;
GN Name=tagE; Synonyms=gtaA, rodD; OrderedLocusNames=BSU35730;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=2507871; DOI=10.1111/j.1365-2958.1989.tb00276.x;
RA Honeyman A.L., Stewart G.C.;
RT "The nucleotide sequence of the rodC operon of Bacillus subtilis.";
RL Mol. Microbiol. 3:1257-1268(1989).
RN [2]
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 [3]
RP REGULATION BY WALR/WALK.
RX PubMed=12950927; DOI=10.1046/j.1365-2958.2003.03661.x;
RA Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T.,
RA Devine K.;
RT "Genes controlled by the essential YycG/YycF two-component system of
RT Bacillus subtilis revealed through a novel hybrid regulator approach.";
RL Mol. Microbiol. 49:1639-1655(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / EB6;
RX PubMed=21558268; DOI=10.1074/jbc.m111.241265;
RA Allison S.E., D'Elia M.A., Arar S., Monteiro M.A., Brown E.D.;
RT "Studies of the genetics, function, and kinetic mechanism of TagE, the wall
RT teichoic acid glycosyltransferase in Bacillus subtilis 168.";
RL J. Biol. Chem. 286:23708-23716(2011).
CC -!- FUNCTION: Catalyzes the addition of glucose to the C-2 hydroxy group of
CC the glycerol units in teichoic acid. {ECO:0000269|PubMed:21558268}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-{[(2R)-1-glycerylphospho](n)-(2R)-1-glycerylphospho}-N-
CC acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl
CC undecaprenyl diphosphate + n UDP-alpha-D-glucose = 4-O-{[(2R)-2-
CC alpha-D-glucosyl-1-glycerylphospho](n)-(2R)-1-glycerylphospho}-N-
CC acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl
CC undecaprenyl diphosphate + n H(+) + n UDP; Xref=Rhea:RHEA:15845,
CC Rhea:RHEA-COMP:12597, Rhea:RHEA-COMP:12614, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:132224,
CC ChEBI:CHEBI:132356; EC=2.4.1.52;
CC Evidence={ECO:0000269|PubMed:21558268};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=770 uM for UDP-alpha-D-glucose {ECO:0000269|PubMed:21558268};
CC KM=23 uM for (GroP)n-ManNAc-beta-(1->4)-GlcNAc-undecaprenyl
CC diphosphate where n=5 {ECO:0000269|PubMed:21558268};
CC KM=4.4 uM for (GroP)n-ManNAc-beta-(1->4)-GlcNAc-undecaprenyl
CC diphosphate where n=40 {ECO:0000269|PubMed:21558268};
CC Note=kcat is 17 sec(-1). {ECO:0000269|PubMed:21558268};
CC -!- PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic acid
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Positively regulated by WalR. Mainly expressed during
CC exponential growth and rapidly shut off as cells enter the stationary
CC phase.
CC -!- DISRUPTION PHENOTYPE: Not essential. No glucose groups on the glycerol
CC residues of teichoic acid in cell walls. {ECO:0000269|PubMed:21558268}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; X15200; CAA33270.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15590.1; -; Genomic_DNA.
DR PIR; S06048; S06048.
DR RefSeq; NP_391454.1; NC_000964.3.
DR RefSeq; WP_003243517.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P13484; -.
DR SMR; P13484; -.
DR IntAct; P13484; 2.
DR STRING; 224308.BSU35730; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; P13484; -.
DR PaxDb; P13484; -.
DR PRIDE; P13484; -.
DR EnsemblBacteria; CAB15590; CAB15590; BSU_35730.
DR GeneID; 936804; -.
DR KEGG; bsu:BSU35730; -.
DR PATRIC; fig|224308.179.peg.3868; -.
DR eggNOG; COG0438; Bacteria.
DR OMA; FFITEEQ; -.
DR PhylomeDB; P13484; -.
DR BioCyc; BSUB:BSU35730-MON; -.
DR BioCyc; MetaCyc:BSU35730-MON; -.
DR UniPathway; UPA00827; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0047265; F:poly(glycerol-phosphate) alpha-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR015397; Glyco_trans_A_1.
DR Pfam; PF09318; Glyco_trans_A_1; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Cytoplasm; Glycosyltransferase;
KW Phosphoprotein; Reference proteome; Teichoic acid biosynthesis;
KW Transferase.
FT CHAIN 1..673
FT /note="Poly(glycerol-phosphate) alpha-glucosyltransferase"
FT /id="PRO_0000080308"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
SQ SEQUENCE 673 AA; 78304 MW; 6E8F6111553F7773 CRC64;
MSLHAVSESN IKQIPDMDYY FISGGLPSNY GGLTKSLLLR SKLFGEECNQ NTFFLTFRFD
LELSSKIDEL YSNGKIDKKF TSVINLFDDF LSVRTNGKRS YEERIGLDQI KKQVGMGKFA
KTLLRLFGKK NNEMSVVYYG DGETIRYVDY WNDKNQLIKR EEYTKNGNLV LVTHYDVQLN
KMYLQEYIND QNQVYLDKLY VWNNEEKDVQ LSHIIWYSLE GEIKVKDESE LRQYWIEYLQ
KQNDKPKLFL VDSRPQDKHV FKVKKSPSSY YGAIIHNKHY GSNKYQIKGR YKEVFSQMYN
LDAVFFITEE QLEDFKLISG EQETFFFTPH TIDKPLDPAV LNVPSEKYKA VIISRLASMK
NLIHAVKAFS LVVKEIPEAK LDIFGSGEDF EKIKKEIEDT KLQNNVFLKG YTDNPDSEFQ
KAWLTISTSH FEGFGLSNME ALSNGCPVVT YDYDYGARSL VTDGANGYVI EQYNIEKLGQ
AIISLMKDES THQKFSEQAF KMAEKYSRPN YIENWAFALN QMIEVRIERE KFSKKVGKKD
PSISSYTEDF DKTKIEIDIE NFDHNDIKKI RLVGLDRKNK AEIISTNLQN DQLFVIDLEK
DVNIEKIAAN KTQVIDFYIV FNANGHIKTM RRLSSEETKL SGNSIDTNNG YRVEPYTTVK
GNFSWRVTEI KES
