ID   TUAG_BACSU              Reviewed;         252 AA.
AC   O32268;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative teichuronic acid biosynthesis glycosyltransferase TuaG;
DE            EC=2.4.-.-;
GN   Name=tuaG; Synonyms=yvhG; OrderedLocusNames=BSU35550;
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=10048024; DOI=10.1046/j.1365-2958.1999.01218.x;
RA   Soldo B., Lazarevic V., Pagni M., Karamata D.;
RT   "Teichuronic acid operon of Bacillus subtilis 168.";
RL   Mol. Microbiol. 31:795-805(1999).
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).
CC   -!- PATHWAY: Cell wall biogenesis; teichuronic acid biosynthesis.
CC   -!- INDUCTION: By phosphate starvation, via the PhoP/PhoR two-component
CC       regulatory system.
CC   -!- MISCELLANEOUS: The nature of the anionic polymer present in the cell
CC       wall of B.subtilis depends on phosphate availability. Under phosphate-
CC       replete growth conditions teichoic acids are present, whereas under
CC       phosphate-depleted conditions, at least part of the wall teichoic acid
CC       is replaced with teichuronic acid, a non-phosphate containing anionic
CC       polymer. The synthesis of teichuronic acid is accompanied by
CC       degradation of teichoic acid and reutilization of liberated phosphate
CC       for other cellular processes such as nucleic acid synthesis.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AF015609; AAB94868.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15572.1; -; Genomic_DNA.
DR   PIR; A69728; A69728.
DR   RefSeq; NP_391435.1; NC_000964.3.
DR   RefSeq; WP_003242619.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32268; -.
DR   SMR; O32268; -.
DR   STRING; 224308.BSU35550; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PaxDb; O32268; -.
DR   PRIDE; O32268; -.
DR   DNASU; 937965; -.
DR   EnsemblBacteria; CAB15572; CAB15572; BSU_35550.
DR   GeneID; 937965; -.
DR   KEGG; bsu:BSU35550; -.
DR   PATRIC; fig|224308.179.peg.3846; -.
DR   eggNOG; COG1215; Bacteria.
DR   InParanoid; O32268; -.
DR   OMA; CLTVMID; -.
DR   PhylomeDB; O32268; -.
DR   BioCyc; BSUB:BSU35550-MON; -.
DR   BioCyc; MetaCyc:BSU35550-MON; -.
DR   UniPathway; UPA00844; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0050845; P:teichuronic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..252
FT                   /note="Putative teichuronic acid biosynthesis
FT                   glycosyltransferase TuaG"
FT                   /id="PRO_0000059229"
SQ   SEQUENCE   252 AA;  29345 MW;  094EC512C5D7A305 CRC64;
     MTNWKPLVSV ITPSYNARDY IEDTVHSVLD QSHPHWEMII VDDCSTDGTR DILQQYEKID
     ERIHVVYLEE NSGAAVARNK ALERAQGRYV AFLDSDDKWK KDKLEKQLEF MMERSCAFSF
     TGYSLMAQDG TPLDKFIHAP ESLTYDDALK NTIIGCLTVM IDREQTGQIQ MPNIRTRQDL
     ATWLSLLKKG FTAYGMNECL AEYRLVNNSI SSNKWKAAKK TWFVYREIER LHFMKATWCF
     VQYAKNAVKK RL