ID   TARA_STAA8              Reviewed;         254 AA.
AC   Q2G2L3;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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, ECO:0000269|PubMed:18215769};
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 {ECO:0000303|PubMed:19376878};
GN   OrderedLocusNames=SAOUHSC_00640 {ECO:0000312|EMBL:ABD29775.1};
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=NCTC 8325 / PS 47;
RX   PubMed=18215769; DOI=10.1016/j.chembiol.2007.11.011;
RA   Brown S., Zhang Y.H., Walker S.;
RT   "A revised pathway proposed for Staphylococcus aureus wall teichoic acid
RT   biosynthesis based on in vitro reconstitution of the intracellular steps.";
RL   Chem. Biol. 15:12-21(2008).
RN   [3]
RP   DISRUPTION PHENOTYPE, AND PATHWAY.
RC   STRAIN=RN4220 / SA178RI;
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:18215769}.
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:18215769};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis. {ECO:0000269|PubMed:18215769,
CC       ECO:0000305|PubMed:19376878}.
CC   -!- DISRUPTION PHENOTYPE: Not essential. 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}.
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DR   EMBL; CP000253; ABD29775.1; -; Genomic_DNA.
DR   RefSeq; WP_000215388.1; NZ_LS483365.1.
DR   RefSeq; YP_499200.1; NC_007795.1.
DR   AlphaFoldDB; Q2G2L3; -.
DR   SMR; Q2G2L3; -.
DR   STRING; 1280.SAXN108_0702; -.
DR   CAZy; GT26; Glycosyltransferase Family 26.
DR   EnsemblBacteria; ABD29775; ABD29775; SAOUHSC_00640.
DR   GeneID; 3920048; -.
DR   KEGG; sao:SAOUHSC_00640; -.
DR   PATRIC; fig|93061.5.peg.574; -.
DR   eggNOG; COG1922; Bacteria.
DR   HOGENOM; CLU_063203_3_1_9; -.
DR   OMA; PWRWRRM; -.
DR   BioCyc; MetaCyc:MON-19984; -.
DR   UniPathway; UPA00790; -.
DR   PRO; PR:Q2G2L3; -.
DR   Proteomes; UP000008816; 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..254
FT                   /note="N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-
FT                   beta-D-mannosaminyltransferase"
FT                   /id="PRO_0000437525"
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