TAGA_BACSU
ID TAGA_BACSU Reviewed; 256 AA.
AC P27620;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070, ECO:0000305};
DE EC=2.4.1.187 {ECO:0000255|HAMAP-Rule:MF_02070, ECO:0000269|PubMed:16953575, ECO:0000269|PubMed:17163636, ECO:0000269|PubMed:2977387};
DE AltName: Full=Major teichoic acid biosynthesis protein A {ECO:0000305};
DE AltName: Full=N-acetylmannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070, ECO:0000305};
DE AltName: Full=UDP-N-acetylmannosamine transferase {ECO:0000255|HAMAP-Rule:MF_02070, ECO:0000305};
DE AltName: Full=UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070, ECO:0000303|PubMed:2977387};
GN Name=tagA {ECO:0000303|PubMed:1906926}; OrderedLocusNames=BSU35750;
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=1906926; DOI=10.1099/00221287-137-4-929;
RA Maueel C., Young M., Karamata D.;
RT "Genes concerned with synthesis of poly(glycerol phosphate), the essential
RT teichoic acid in Bacillus subtilis strain 168, are organized in two
RT divergent transcription units.";
RL J. Gen. Microbiol. 137:929-941(1991).
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=AHU 1035;
RX PubMed=2977387; DOI=10.1093/oxfordjournals.jbchem.a122594;
RA Murazumi N., Kumita K., Araki Y., Ito E.;
RT "Partial purification and properties of UDP-N-acetylmannosamine:N-
RT acetylglucosaminyl pyrophosphorylundecaprenol N-
RT acetylmannosaminyltransferase from Bacillus subtilis.";
RL J. Biochem. 104:980-984(1988).
RN [4]
RP FUNCTION.
RX PubMed=11882717; DOI=10.1099/00221287-148-3-815;
RA Lazarevic V., Abellan F.-X., Beggah Moeller S., Karamata D., Maueel C.;
RT "Comparison of ribitol and glycerol teichoic acid genes in Bacillus
RT subtilis W23 and 168: identical function, similar divergent organization,
RT but different regulation.";
RL Microbiology 148:815-824(2002).
RN [5]
RP REGULATION BY WALR/WALK.
RX PubMed=12950927; DOI=10.1046/j.1365-2958.2003.03661.x;
RA Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T.,
RA Devine K.;
RT "Genes controlled by the essential YycG/YycF two-component system of
RT Bacillus subtilis revealed through a novel hybrid regulator approach.";
RL Mol. Microbiol. 49:1639-1655(2003).
RN [6]
RP CATALYTIC ACTIVITY.
RC STRAIN=168 / PY79;
RX PubMed=17163636; DOI=10.1021/cb0500041;
RA Ginsberg C., Zhang Y.H., Yuan Y., Walker S.;
RT "In vitro reconstitution of two essential steps in wall teichoic acid
RT biosynthesis.";
RL ACS Chem. Biol. 1:25-28(2006).
RN [7]
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND REACTION MECHANISM.
RC STRAIN=168 / EB6;
RX PubMed=16953575; DOI=10.1021/bi060872z;
RA Zhang Y.H., Ginsberg C., Yuan Y., Walker S.;
RT "Acceptor substrate selectivity and kinetic mechanism of Bacillus subtilis
RT TagA.";
RL Biochemistry 45:10895-10904(2006).
RN [8]
RP DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=168 / EB6;
RX PubMed=19376878; DOI=10.1128/jb.00611-08;
RA D'Elia M.A., Henderson J.A., Beveridge T.J., Heinrichs D.E., Brown E.D.;
RT "The N-acetylmannosamine transferase catalyzes the first committed step of
RT teichoic acid assembly in Bacillus subtilis and Staphylococcus aureus.";
RL J. Bacteriol. 191:4030-4034(2009).
CC -!- FUNCTION: Catalyzes the conversion of GlcNAc-PP-undecaprenol into
CC ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate
CC in the de novo synthesis of teichoic acid. {ECO:0000255|HAMAP-
CC Rule:MF_02070, ECO:0000269|PubMed:11882717,
CC ECO:0000269|PubMed:2977387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl
CC diphosphate + UDP-N-acetyl-alpha-D-mannosamine = H(+) + N-acetyl-
CC beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-
CC trans,octa-cis-undecaprenyl diphosphate + UDP; Xref=Rhea:RHEA:16053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:62959,
CC ChEBI:CHEBI:68623, ChEBI:CHEBI:132210; EC=2.4.1.187;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02070,
CC ECO:0000269|PubMed:16953575, ECO:0000269|PubMed:17163636,
CC ECO:0000269|PubMed:2977387};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for UDP-N-acetyl-alpha-D-mannosamine
CC {ECO:0000269|PubMed:2977387};
CC Vmax=1.5 nmol/h/mg enzyme {ECO:0000269|PubMed:2977387};
CC pH dependence:
CC Optimum pH is 7-7.5. {ECO:0000269|PubMed:2977387};
CC -!- PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic acid
CC biosynthesis. {ECO:0000269|PubMed:19376878}.
CC -!- INDUCTION: Positively regulated by WalR. Mainly expressed during
CC exponential growth and rapidly shut off as cells enter the stationary
CC phase. {ECO:0000269|PubMed:12950927}.
CC -!- DISRUPTION PHENOTYPE: Not essential. Impaired growth. Looses rod shape
CC of cells. No teichoic acid in cell walls.
CC {ECO:0000269|PubMed:19376878}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 26 family. TagA/TarA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02070, ECO:0000305}.
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DR EMBL; M57497; AAA22844.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15592.1; -; Genomic_DNA.
DR PIR; B49757; B49757.
DR RefSeq; NP_391456.1; NC_000964.3.
DR RefSeq; WP_003227919.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P27620; -.
DR SMR; P27620; -.
DR IntAct; P27620; 7.
DR STRING; 224308.BSU35750; -.
DR CAZy; GT26; Glycosyltransferase Family 26.
DR PaxDb; P27620; -.
DR PRIDE; P27620; -.
DR DNASU; 936810; -.
DR EnsemblBacteria; CAB15592; CAB15592; BSU_35750.
DR GeneID; 936810; -.
DR KEGG; bsu:BSU35750; -.
DR PATRIC; fig|224308.179.peg.3870; -.
DR eggNOG; COG1922; Bacteria.
DR InParanoid; P27620; -.
DR OMA; PWRWRRM; -.
DR PhylomeDB; P27620; -.
DR BioCyc; BSUB:BSU35750-MON; -.
DR BioCyc; MetaCyc:BSU35750-MON; -.
DR SABIO-RK; P27620; -.
DR UniPathway; UPA00827; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR GO; GO:0047244; F:N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06533; Glyco_transf_WecG_TagA; 1.
DR HAMAP; MF_02070; TagA_TarA; 1.
DR InterPro; IPR034714; TagA_TarA.
DR InterPro; IPR004629; WecG_TagA_CpsF.
DR PANTHER; PTHR34136; PTHR34136; 1.
DR Pfam; PF03808; Glyco_tran_WecG; 1.
DR TIGRFAMs; TIGR00696; wecG_tagA_cpsF; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Reference proteome;
KW Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..256
FT /note="N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-
FT beta-D-mannosaminyltransferase"
FT /id="PRO_0000208438"
SQ SEQUENCE 256 AA; 29499 MW; 2447ECA7E0C0B167 CRC64;
MQTETIHNIP YVNSNLTSFI DYLEKHYIDQ KIGAVISTVN PEIAFAAIKD RDYFDVLSSS
NFILPDGIGV VMMSRLTNNR LQSRIAGYDV FKELLGVANK KKKRIFLYGA KKDVIKGVVS
KISSEYPNIK IAGYSDGYVQ DRTLVAKQIA RANPDMVFVA LGYPHQEKFI HNYRHLFPKA
VSIGLGGSFD VFSGNVKRAP SWMIRLNLEW FYRLILNPWR WKRMLSIPKY ALTVLKEEKN
KKTFYPKPEK DHTKQI
