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Database: UniProt
Entry: V7HUM9_9LACO
LinkDB: V7HUM9_9LACO
Original site: V7HUM9_9LACO 
ID   V7HUM9_9LACO            Unreviewed;       243 AA.
AC   V7HUM9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=LEQ_0815c {ECO:0000313|EMBL:ETA73904.1};
OS   Ligilactobacillus equi DPC 6820.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1392007 {ECO:0000313|EMBL:ETA73904.1, ECO:0000313|Proteomes:UP000018559};
RN   [1] {ECO:0000313|EMBL:ETA73904.1, ECO:0000313|Proteomes:UP000018559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 6820 {ECO:0000313|EMBL:ETA73904.1,
RC   ECO:0000313|Proteomes:UP000018559};
RX   PubMed=24435863;
RA   O'Donnell M.M., Harris H.M., O'Toole P.W., Ross R.P.;
RT   "The Genome of the Predominant Equine Lactobacillus Species, Lactobacillus
RT   equi, Is Reflective of Its Lifestyle Adaptations to an Herbivorous Host.";
RL   Genome Announc. 2:e01155-e01113(2014).
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:ETA73904.1}.
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DR   EMBL; AWWH01000140; ETA73904.1; -; Genomic_DNA.
DR   RefSeq; WP_023859869.1; NZ_AWWH01000140.1.
DR   AlphaFoldDB; V7HUM9; -.
DR   PATRIC; fig|1392007.3.peg.1281; -.
DR   UniPathway; UPA00632; -.
DR   Proteomes; UP000018559; 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   Reference proteome {ECO:0000313|Proteomes:UP000018559};
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:ETA73904.1}.
SQ   SEQUENCE   243 AA;  27458 MW;  837E1B10CFFE43ED CRC64;
     MSKFQTVSVL GVDFIKATNA EFLQALFNDS LQRKNRFVVT ANPEIVLAAK NDPAYYQTLK
     TADYITADGI GIIKGAKILG TPLPERVTGY DTMLKLLEFA NQEAKKVFLV GGKPDVIQKA
     REKILQTYPH IKIVGAYDGY FKDDKEITQA IAQSQPDFVF AALGFPKQEN FIAKNRQLAS
     AIWMGVGGSF DVLAGTVKRA PNFWIKLNLE WFYRLLKEPT RFKRMLALPR YLSLVKKEAK
     RQK
//
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