TUAE_BACSU
ID TUAE_BACSU Reviewed; 488 AA.
AC O32270;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Teichuronic acid biosynthesis protein TuaE;
GN Name=tuaE; Synonyms=yvhE; OrderedLocusNames=BSU35570;
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 polymerization of teichuronic acid
CC repeating units after their translocation to the outer surface of the
CC 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.
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DR EMBL; AF015609; AAB94866.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15574.1; -; Genomic_DNA.
DR PIR; G69727; G69727.
DR RefSeq; NP_391437.1; NC_000964.3.
DR RefSeq; WP_010886625.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32270; -.
DR STRING; 224308.BSU35570; -.
DR PaxDb; O32270; -.
DR PRIDE; O32270; -.
DR EnsemblBacteria; CAB15574; CAB15574; BSU_35570.
DR GeneID; 936765; -.
DR KEGG; bsu:BSU35570; -.
DR PATRIC; fig|224308.179.peg.3848; -.
DR eggNOG; COG3307; Bacteria.
DR InParanoid; O32270; -.
DR OMA; YKQHYPT; -.
DR BioCyc; BSUB:BSU35570-MON; -.
DR BioCyc; MetaCyc:BSU35570-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; IPR007016; O-antigen_ligase-related.
DR Pfam; PF04932; Wzy_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..488
FT /note="Teichuronic acid biosynthesis protein TuaE"
FT /id="PRO_0000065691"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..476
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 488 AA; 55536 MW; 44925BC675AFD885 CRC64;
MSIKRSAVHT LALLAAAIFG VVLLLGAIHK DIGFMQMAAV LAVLAIGLFL LTLATAFTTK
ERLFMAVIYI LIACTFLNNA FFAIHLGFFS LFLYRLLLIA AGCLHIFGMV RNRTHIERWH
GLQVKGILLF FAFWFIYGLV SLLWAKSVTV GLKYLALLAM GIFFIYLIVM YVQKMERLMI
VYAIWLVMTV FLMIIGFYNH ITHHHLASST LYSGPEYKQH YPTSVFFNQN DFATFLSISF
FFYITMMKNI KNGYIKAIGL VLSLCALYLI FATGSRASLL GIFAGIAVYI FIVLPPVLKR
MAIWLSAAGI ALFAVLFASK IYSKFWELFL APQTLHSFHD RLPSNVARAN LLKNAWHFFL
DSYGFGVGAG NVSYYLEHYA VYDTDNVAEV HNWLVEILAN FGLFIMLGYL SVYAYLIWVL
YKFYERKLEN QSKLITEGLI TAMVSFLVSS ISPSSVSNLF FHWVFMALVI AAVNVLRRSR
QMPEPMYR
