ID   TUAF_BACSU              Reviewed;         226 AA.
AC   O32269;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Teichuronic acid biosynthesis protein TuaF;
GN   Name=tuaF; Synonyms=yvhF; OrderedLocusNames=BSU35560;
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   -!- 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.
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DR   EMBL; AF015609; AAB94867.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15573.1; -; Genomic_DNA.
DR   PIR; H69727; H69727.
DR   RefSeq; NP_391436.1; NC_000964.3.
DR   RefSeq; WP_003243110.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32269; -.
DR   SMR; O32269; -.
DR   STRING; 224308.BSU35560; -.
DR   PaxDb; O32269; -.
DR   PRIDE; O32269; -.
DR   EnsemblBacteria; CAB15573; CAB15573; BSU_35560.
DR   GeneID; 936768; -.
DR   KEGG; bsu:BSU35560; -.
DR   PATRIC; fig|224308.179.peg.3847; -.
DR   eggNOG; COG3206; Bacteria.
DR   OMA; YELKNTQ; -.
DR   BioCyc; BSUB:BSU35560-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:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0050845; P:teichuronic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR003856; LPS_length_determ_N_term.
DR   Pfam; PF02706; Wzz; 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..226
FT                   /note="Teichuronic acid biosynthesis protein TuaF"
FT                   /id="PRO_0000065692"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   226 AA;  25135 MW;  3039AC97353BBB69 CRC64;
     MNDILIRIAR RIKKNIIWII AVPIILGAAG YILPSQIADQ KSYTAEDTLA VGSYDHPVYN
     STEEIPLLLK SDSFLKEALP DEKDEDVAEI KEKLTINTES KSLLTLSYSD EDKDRTESVL
     NAISSTFLKN DQKLYAEREA VIRSSIDALE GESVSEDSKV DKERFLYELK NTQLNLKAAS
     VTDSETVSET AGGGMSPKKK AVLGVMIGLT IAFMFVVIPE FFRESF