ID   TUAH_BACSU              Reviewed;         397 AA.
AC   O32267;
DT   20-JUN-2003, 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 TuaH;
DE            EC=2.4.-.-;
GN   Name=tuaH; Synonyms=yvhH; OrderedLocusNames=BSU35540;
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       {ECO:0000305}.
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DR   EMBL; AF015609; AAB94869.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15571.1; -; Genomic_DNA.
DR   PIR; B69728; B69728.
DR   RefSeq; NP_391434.1; NC_000964.3.
DR   RefSeq; WP_003243252.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32267; -.
DR   SMR; O32267; -.
DR   STRING; 224308.BSU35540; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PaxDb; O32267; -.
DR   PRIDE; O32267; -.
DR   DNASU; 938535; -.
DR   EnsemblBacteria; CAB15571; CAB15571; BSU_35540.
DR   GeneID; 938535; -.
DR   KEGG; bsu:BSU35540; -.
DR   PATRIC; fig|224308.43.peg.3720; -.
DR   eggNOG; COG0438; Bacteria.
DR   InParanoid; O32267; -.
DR   OMA; YYCGDDF; -.
DR   PhylomeDB; O32267; -.
DR   BioCyc; BSUB:BSU35540-MON; -.
DR   BioCyc; MetaCyc:BSU35540-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.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..397
FT                   /note="Putative teichuronic acid biosynthesis
FT                   glycosyltransferase TuaH"
FT                   /id="PRO_0000080310"
SQ   SEQUENCE   397 AA;  45591 MW;  E1D19BC8033E5B72 CRC64;
     METKEAIIHV IVATAEWGKD QLRYRRHRLA EFLAAQEETK EVIWVCPAPR AQGKEFQEVH
     SGIRQFAVKD LLQKKMFRFG RYTDVFYRHK LSPLLDELTP ASANGERCCL WYTFPGFPLL
     SSLYSWDQVI YDCSDLWAAP ISGRSNLLSE FRRKVIKSAE LRIIQRADSI TCSSDYLHKE
     VDKKLTAGRE KVHTVENGVE YELFSANKQA PDRSILQGRE GIVLGFIGGI KPKLDFKMIK
     EAALQKPDWT FLWVGPDATN GDVSFQELLR LPNVIWTGPA DPKEVPHYME LIDIGIMPYK
     QSPYNQAVFP LKLFEFLAAG KPVVGTNLPS TSKMQKPYVY EYVEGDHPID FIAACEKVLG
     QNGDETYKEM RRNIARTQDW NCLFRQIMKY TGIQKHA