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Database: UniProt
Entry: A0A0E4HED2_9BACL
LinkDB: A0A0E4HED2_9BACL
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ID   A0A0E4HED2_9BACL        Unreviewed;       251 AA.
AC   A0A0E4HED2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE            EC=2.4.1.187 {ECO:0000256|HAMAP-Rule:MF_02070};
DE   AltName: Full=N-acetylmannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE   AltName: Full=UDP-N-acetylmannosamine transferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE   AltName: Full=UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
GN   ORFNames=PRIO_6299 {ECO:0000313|EMBL:CQR58646.1};
OS   Paenibacillus riograndensis SBR5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC   Paenibacillus sonchi group.
OX   NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR58646.1, ECO:0000313|Proteomes:UP000033163};
RN   [1] {ECO:0000313|Proteomes:UP000033163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_02070};
CC   -!- PATHWAY: Cell wall biogenesis; teichoic acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02070}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 26 family. TagA/TarA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_02070}.
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DR   EMBL; LN831776; CQR58646.1; -; Genomic_DNA.
DR   RefSeq; WP_039788282.1; NZ_LN831776.1.
DR   AlphaFoldDB; A0A0E4HED2; -.
DR   STRING; 483937.AMQ84_22230; -.
DR   KEGG; pri:PRIO_6299; -.
DR   PATRIC; fig|1073571.4.peg.6732; -.
DR   HOGENOM; CLU_063203_3_1_9; -.
DR   UniPathway; UPA00632; -.
DR   Proteomes; UP000033163; Chromosome I.
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   NCBIfam; TIGR00696; wecG_tagA_cpsF; 1.
DR   PANTHER; PTHR34136; -; 1.
DR   PANTHER; PTHR34136:SF1; UDP-N-ACETYL-D-MANNOSAMINURONIC ACID TRANSFERASE; 1.
DR   Pfam; PF03808; Glyco_tran_WecG; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02070};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
KW   Teichoic acid biosynthesis {ECO:0000256|ARBA:ARBA00022944,
KW   ECO:0000256|HAMAP-Rule:MF_02070};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02070, ECO:0000313|EMBL:CQR58646.1}.
SQ   SEQUENCE   251 AA;  28254 MW;  61576549C8961B26 CRC64;
     MKAESVIPTV PIFGIRVSRV DMKATVSYLT EAVQRREPHQ VITANPIMVM TALDNPAYME
     IMKSAELVVP DGTGVVWAAE YCQQPVAERV AGFDLLHELL HQGESYNWRV YLLGSTPEVI
     RETASRLQSQ YAGIIIAGYH DGFFGPEADE EIVSEIIEAQ PDLLFVARGA DSQEPWIAKY
     KSRLNIPVMM GVGGSFDVIS GKSRRAPKAF QKLRAEWLYR LLKEPTRYKR MLALPKFAVK
     VLREKDKVTK V
//
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