ID   TUAB_BACSU              Reviewed;         483 AA.
AC   O32273;
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=Teichuronic acid biosynthesis protein TuaB;
GN   Name=tuaB; Synonyms=yvhB; OrderedLocusNames=BSU35600;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PUTATIVE FUNCTION.
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   -!- FUNCTION: Might be involved in the translocation of teichuronic acid
CC       repeating units from the inner to the outer surface of the membrane.
CC   -!- PATHWAY: Cell wall biogenesis; teichuronic acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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 polysaccharide synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AF015609; AAB94863.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15577.1; -; Genomic_DNA.
DR   PIR; D69727; D69727.
DR   RefSeq; NP_391440.1; NC_000964.3.
DR   RefSeq; WP_003244371.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32273; -.
DR   SMR; O32273; -.
DR   STRING; 224308.BSU35600; -.
DR   TCDB; 2.A.66.2.6; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR   PaxDb; O32273; -.
DR   PRIDE; O32273; -.
DR   EnsemblBacteria; CAB15577; CAB15577; BSU_35600.
DR   GeneID; 936770; -.
DR   KEGG; bsu:BSU35600; -.
DR   PATRIC; fig|224308.179.peg.3851; -.
DR   eggNOG; COG2244; Bacteria.
DR   InParanoid; O32273; -.
DR   OMA; DLAFYWD; -.
DR   PhylomeDB; O32273; -.
DR   BioCyc; BSUB:BSU35600-MON; -.
DR   BioCyc; MetaCyc:BSU35600-MON; -.
DR   UniPathway; UPA00844; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR029303; Polysacc_synt_C.
DR   InterPro; IPR002797; Polysacc_synth.
DR   Pfam; PF01943; Polysacc_synt; 1.
DR   Pfam; PF14667; Polysacc_synt_C; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW   Reference proteome; Stress response; Transmembrane; Transmembrane helix.
FT   CHAIN           1..483
FT                   /note="Teichuronic acid biosynthesis protein TuaB"
FT                   /id="PRO_0000166452"
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   483 AA;  53720 MW;  FDBC6D11CFA8FCEF CRC64;
     MPSITKQIMS GAKWTSISTM CITIIQIVQF ALLGNMMTLT EFGLVGMITT VTVFAQIVLD
     MGFGAALIQR DDATERQLST LYWLNIMTGV LLFVLLYVSS PVIAGFYQRE ELVFLVRILA
     IMFLIAPIGQ QYQYMLQKQL HFNTLSKIEI FSNVLSFGYL AIAVFMMDAI LAYVISQVLL
     QSSKGILYWA VYRKKWHPAF VFDLRGMKDF FSFGAFQLSS RLVNRLGANI DMILIGRFIG
     AEALGIYNLA YQIVTIPVLK INPIVTRVAF PIFAKNKYEN SVIREGFLNM TKMLALVSFP
     LLIGLVSVSD AFITAVFGEK WLAAVPILNV LAIVGILRVL MNPNGSVLLA KGRADLAFYW
     DSGVLLLYGL SLFAAVQTGS LLTVAWVYAI ISVVNFLIGR WLLAYVIKLN LSAYFQSIMK
     PFLITAAMGI IAFGVSLSTE HFSMQAEMRL AISVAAGALC YLFLLVKAYP QTKSKLLRKG
     RLS