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Database: UniProt
Entry: A0A137SWU5_9FIRM
LinkDB: A0A137SWU5_9FIRM
Original site: A0A137SWU5_9FIRM 
ID   A0A137SWU5_9FIRM        Unreviewed;       253 AA.
AC   A0A137SWU5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=HMPREF3189_00382 {ECO:0000313|EMBL:KXO16928.1};
OS   Clostridiales bacterium KA00134.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1588750 {ECO:0000313|EMBL:KXO16928.1, ECO:0000313|Proteomes:UP000070500};
RN   [1] {ECO:0000313|EMBL:KXO16928.1, ECO:0000313|Proteomes:UP000070500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00134 {ECO:0000313|EMBL:KXO16928.1,
RC   ECO:0000313|Proteomes:UP000070500};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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}.
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:KXO16928.1}.
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DR   EMBL; LTAF01000006; KXO16928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137SWU5; -.
DR   STRING; 1588750.HMPREF3189_00382; -.
DR   PATRIC; fig|1588750.3.peg.375; -.
DR   OrthoDB; 9771846at2; -.
DR   UniPathway; UPA00632; -.
DR   Proteomes; UP000070500; 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:UP000070500};
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:KXO16928.1}.
SQ   SEQUENCE   253 AA;  28575 MW;  03AC88582A1ABB74 CRC64;
     MTRNKISIFG VEILNVTFEE SAKILKEFLQ ENKLHTIVTP NTEIVMACKK DEKLKNLIND
     QDLVIPDGIG LVIGSKIRKK PLKERVTGFD ISMELIKIAH EEGYSLYLLG GEPGIALQAQ
     KKLQESFPGL DIVGTQHGYF KGTHLGQKGH PEELAVIADI NEKKPDIIFL GLGFPKQEIW
     IEEYRNKLKS KIIIGNGGVL DVIAGKSKRA PEIFIKLNLE WLYRLLKDPS RIKRQMAIPK
     FLFSIMTDKD AVK
//
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