ID V5E0D2_9LACO Unreviewed; 243 AA.
AC V5E0D2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=Lc367_0418 {ECO:0000313|EMBL:EST03586.1};
OS Lactobacillus crispatus EM-LC1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1328863 {ECO:0000313|EMBL:EST03586.1, ECO:0000313|Proteomes:UP000017999};
RN [1] {ECO:0000313|EMBL:EST03586.1, ECO:0000313|Proteomes:UP000017999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM-LC1 {ECO:0000313|EMBL:EST03586.1,
RC ECO:0000313|Proteomes:UP000017999};
RX PubMed=24356836;
RA Power S.E., Harris H.M., Bottacini F., Ross R.P., O'Toole P.W.,
RA Fitzgerald G.F.;
RT "Draft Genome Sequence of Lactobacillus crispatus EM-LC1, an Isolate with
RT Antimicrobial Activity Cultured from an Elderly Subject.";
RL Genome Announc. 1:e01070-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EST03586.1}.
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DR EMBL; AXLM01000015; EST03586.1; -; Genomic_DNA.
DR RefSeq; WP_023488291.1; NZ_AXLM01000015.1.
DR AlphaFoldDB; V5E0D2; -.
DR PATRIC; fig|1328863.3.peg.894; -.
DR UniPathway; UPA00632; -.
DR Proteomes; UP000017999; Unassembled WGS sequence.
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:EST03586.1}.
SQ SEQUENCE 243 AA; 27586 MW; 73B1F0DA3A9439E6 CRC64;
MSKVNILGVD FDNKTFNQFQ NEFINRLNNH LSTFVVTANP EIVMAANENP EFMKILKNDP
DYITADGIGI VKAAKMLKQP LPERVTGYDL FTWLMDVAND RGSRVYLIGA KPQVIHAVQS
KIAKEYSNIN LVGAEDGYFT EDLELVARRI QKAQPDMVFA ALGFPKQEKL LSILRKNETP
ALMMGVGGSF DVFSGIVKRA PEAFQKTHLE WFYRLITNPS RFKRMLVLPQ FVVRVKQSKK
KGK
//
