TUAA_BACSU
ID TUAA_BACSU Reviewed; 179 AA.
AC O32274;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative undecaprenyl-phosphate N-acetylgalactosaminyl 1-phosphate transferase {ECO:0000305|PubMed:10048024};
DE EC=2.7.8.40 {ECO:0000305|PubMed:10048024};
DE AltName: Full=Teichuronic acid biosynthesis protein TuaA;
DE AltName: Full=UDP-GalNAc:undecaprenyl-P GalNAc-1-P transferase;
GN Name=tuaA; Synonyms=yvhA; OrderedLocusNames=BSU35610;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PUTATIVE FUNCTION, AND INDUCTION.
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 mediate the very first reaction in teichuronic
CC synthesis, i.e. the formation of lipid-linked N-acetylglucosamine.
CC {ECO:0000305|PubMed:10048024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC D-galactosamine = N-acetyl-alpha-D-galactosaminyl-di-trans,octa-cis-
CC undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:36787,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:60392, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:74214; EC=2.7.8.40;
CC Evidence={ECO:0000305|PubMed:10048024};
CC -!- PATHWAY: Cell wall biogenesis; teichuronic acid biosynthesis.
CC {ECO:0000305|PubMed:10048024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By phosphate starvation, via the PhoP/PhoR two-component
CC regulatory system. {ECO:0000269|PubMed:10048024}.
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 {ECO:0000305|PubMed:10048024}.
CC -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC {ECO:0000305}.
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DR EMBL; AF015609; AAB94862.1; -; Genomic_DNA.
DR EMBL; AL009126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C69727; C69727.
DR AlphaFoldDB; O32274; -.
DR SMR; O32274; -.
DR PaxDb; O32274; -.
DR PRIDE; O32274; -.
DR PATRIC; fig|224308.179.peg.3852; -.
DR InParanoid; O32274; -.
DR BioCyc; MetaCyc:MON-20033; -.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; 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; IPR003362; Bact_transf.
DR Pfam; PF02397; Bac_transf; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Stress response; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..179
FT /note="Putative undecaprenyl-phosphate N-
FT acetylgalactosaminyl 1-phosphate transferase"
FT /id="PRO_0000166469"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 179 AA; 20323 MW; 1BB1E620230950EE CRC64;
MSAEKSMNVS REFSVQQIHS FTLSEKTARY LAIKRVMDIW FALIGLAIAL PMIAVFSILI
CLETPGPAIY TQERVGKGGK PFKLYKLRSM KIDAEKSGAV WAQKQDPRVT RIGAFIRRTR
IDELPQLFNV LKGDMSMIGP RPERPVFTEK FQNEIPGFTQ RLGSGERRLR YDAEGKADI
