TARA_STAAW
ID TARA_STAAW Reviewed; 254 AA.
AC Q8NXS7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070};
DE EC=2.4.1.187 {ECO:0000255|HAMAP-Rule:MF_02070};
DE AltName: Full=N-acetylmannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070};
DE AltName: Full=UDP-N-acetylmannosamine transferase {ECO:0000255|HAMAP-Rule:MF_02070};
DE AltName: Full=UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_02070};
GN Name=tarA; OrderedLocusNames=MW0598;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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}.
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 -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 26 family. TagA/TarA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02070}.
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DR EMBL; BA000033; BAB94463.1; -; Genomic_DNA.
DR RefSeq; WP_000215390.1; NC_003923.1.
DR AlphaFoldDB; Q8NXS7; -.
DR SMR; Q8NXS7; -.
DR CAZy; GT26; Glycosyltransferase Family 26.
DR EnsemblBacteria; BAB94463; BAB94463; BAB94463.
DR KEGG; sam:MW0598; -.
DR HOGENOM; CLU_063203_3_1_9; -.
DR OMA; PWRWRRM; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000000418; Chromosome.
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 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Glycosyltransferase;
KW Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..254
FT /note="N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-
FT beta-D-mannosaminyltransferase"
FT /id="PRO_0000208446"
SQ SEQUENCE 254 AA; 29151 MW; 99C014388CFA90FF CRC64;
MTVEERSNTA KVDILGVDFD NTTMLQMVEN IKTFFANQST NNLFIVTANP EIVNYATTHQ
AYLELINQAS YIVADGTGVV KASHRLKQPL AHRIPGIELM DECLKIAHVN HQKVFLLGAT
NEVVEAAQYA LQQRYPNISF AHHHGYIDLE DETVVKRIKL FKPDYIFVGM GFPKQEEWIM
THENQFESTV MMGVGGSLEV FAGAKKRAPY IFRKLNIEWI YRALMDWKRI GRLKSIPIFM
YKIAKAKRKI KKAK
