ID   TARA_STAAU              Reviewed;         254 AA.
AC   Q9LC45;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   25-MAY-2022, entry version 86.
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;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NU3-1;
RX   PubMed=10754251; DOI=10.1111/j.1574-6968.2000.tb09065.x;
RA   Horii T., Yokoyama K., Barua S., Odagiri T., Futamura N., Hasegawa T.,
RA   Ohta M.;
RT   "The staphylokinase gene is located in the structural gene encoding N-
RT   acetylmuramyl-L-alanine amidase in methicillin-resistant Staphylococcus
RT   aureus.";
RL   FEMS Microbiol. Lett. 185:221-224(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA95012.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB033232; BAA95012.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000215388.1; NZ_WYDB01000004.1.
DR   AlphaFoldDB; Q9LC45; -.
DR   SMR; Q9LC45; -.
DR   OMA; PWRWRRM; -.
DR   UniPathway; UPA00790; -.
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_0000208440"
SQ   SEQUENCE   254 AA;  29133 MW;  99C014388CFED0BB CRC64;
     MTVEERSNTA KVDILGVDFD NTTMLQMVEN IKTFFANQST NNLFIVTANP EIVNYATTHQ
     AYLELINQAS YIVADGTGVV KASHRLKQPL AHRIPGIELM DECLKIAHVN HQKVFLLGAT
     NEVVEAAQYA LQQRYPNISF AHHHGYIDLE DETVVKRIKL FKPDYIFVGM GFPKQEEWIM
     THENQFESTV MMGVGGSLEV FAGAKKRAPY IFRKLNIEWI YRALIDWKRI GRLKSIPIFM
     YKIAKAKRKI KKAK