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Database: UniProt
Entry: I9DH74_9FIRM
LinkDB: I9DH74_9FIRM
Original site: I9DH74_9FIRM 
ID   I9DH74_9FIRM            Unreviewed;       241 AA.
AC   I9DH74;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=JBW_02255 {ECO:0000313|EMBL:AJQ27601.1};
OS   Pelosinus fermentans JBW45.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1192197 {ECO:0000313|EMBL:AJQ27601.1, ECO:0000313|Proteomes:UP000005361};
RN   [1] {ECO:0000313|EMBL:AJQ27601.1, ECO:0000313|Proteomes:UP000005361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBW45 {ECO:0000313|EMBL:AJQ27601.1,
RC   ECO:0000313|Proteomes:UP000005361};
RX   PubMed=26404608;
RA   De Leon K.B., Utturkar S.M., Camilleri L.B., Elias D.A., Arkin A.P.,
RA   Fields M.W., Brown S.D., Wall J.D.;
RT   "Complete Genome Sequence of Pelosinus fermentans JBW45, a Member of a
RT   Remarkably Competitive Group of Negativicutes in the Firmicutes Phylum.";
RL   Genome Announc. 3:e01090-e01015(2015).
RN   [2] {ECO:0000313|Proteomes:UP000005361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBW45 {ECO:0000313|Proteomes:UP000005361};
RA   De Leon K.B., Utturkar S.M., Camilleri L.B., Arkin A.P., Fields M.W.,
RA   Brown S.D., Wall J.D.;
RT   "Complete Genome Sequence of Pelosinus fermentans JBW45.";
RL   Submitted (FEB-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; CP010978; AJQ27601.1; -; Genomic_DNA.
DR   RefSeq; WP_007956587.1; NZ_CP010978.1.
DR   AlphaFoldDB; I9DH74; -.
DR   STRING; 1192197.JBW_02255; -.
DR   KEGG; pft:JBW_02255; -.
DR   HOGENOM; CLU_063203_3_1_9; -.
DR   OrthoDB; 9771846at2; -.
DR   UniPathway; UPA00632; -.
DR   Proteomes; UP000005361; Chromosome.
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   ECO:0000313|EMBL:AJQ27601.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005361};
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:AJQ27601.1}.
SQ   SEQUENCE   241 AA;  27131 MW;  73C99A5262EB655A CRC64;
     MRNRIAVLNV MIDVVTMKEA VEAVKQFILQ KKSHLVVTPN PEIIMMANKD EQLARIINNA
     DLVVPDGAGV VWAARYQGDA MPERVAGYDL VQNLLIEAMS EKYKIYLFGG APGIAEKAKK
     IAEERYPGVQ IVGTRNGFFT KQNESEIVND IKACQPDILL VALGVPRQEK WLEEYKEELK
     VPVSIGVGGT FDVMAGVVKR APLWMQRSNL EWLFRLLSEP KRAIRMLALP HFVIKIMTTK
     K
//
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