TUAC_BACSU
ID TUAC_BACSU Reviewed; 389 AA.
AC O32272;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative teichuronic acid biosynthesis glycosyltransferase TuaC;
DE EC=2.4.-.-;
GN Name=tuaC; Synonyms=yvhC; OrderedLocusNames=BSU35590;
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 group 1 family.
CC Glycosyltransferase 4 subfamily. {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; AF015609; AAB94864.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15576.1; -; Genomic_DNA.
DR PIR; E69727; E69727.
DR RefSeq; NP_391439.1; NC_000964.3.
DR RefSeq; WP_003242807.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32272; -.
DR SMR; O32272; -.
DR STRING; 224308.BSU35590; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PaxDb; O32272; -.
DR PRIDE; O32272; -.
DR DNASU; 936771; -.
DR EnsemblBacteria; CAB15576; CAB15576; BSU_35590.
DR GeneID; 936771; -.
DR KEGG; bsu:BSU35590; -.
DR PATRIC; fig|224308.179.peg.3850; -.
DR eggNOG; COG0297; Bacteria.
DR eggNOG; COG0438; Bacteria.
DR InParanoid; O32272; -.
DR OMA; PFADKYE; -.
DR PhylomeDB; O32272; -.
DR BioCyc; BSUB:BSU35590-MON; -.
DR BioCyc; MetaCyc:BSU35590-MON; -.
DR UniPathway; UPA00844; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016758; F:hexosyltransferase 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 InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..389
FT /note="Putative teichuronic acid biosynthesis
FT glycosyltransferase TuaC"
FT /id="PRO_0000080309"
SQ SEQUENCE 389 AA; 43276 MW; 25C3E2511C74B163 CRC64;
MKILWITSVY PSSMKPGEGV FHETQVQELQ KLGLDITVIC PRPFHSAPVR MLKKTYRKKD
VRPEYEIRKG IPVYRPFYRA VPGQLKWAQP HRRIASAVLK TMKQRDLYPD LIHAHFAMPS
GGAAAVVSES AQIPYVLTLH GSDVNVYPHY SKGAFKAFKR AVGSASVVLA VSHKLQEEAK
KLSGFDSSVL PIGIQLSRFQ GNEETKEEIR KRLGLPLDQR LAVYVGRLVR EKGIFELSEA
IESLQDSPKA VFVGDGPAKS TLTQKGHIVT GQVPNHQVRD YLLAADLFVL PSYSEGMPTV
VIEALALRVP VICTDVGGVS SLFGKHQHLL IKPKSAQALA EAITRYEHEQ IWKPEVADDL
YETVQAQFDA GKNAKALHHQ YQTVTKTSV
