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Database: UniProt
Entry: I4DCC8_DESAJ
LinkDB: I4DCC8_DESAJ
Original site: I4DCC8_DESAJ 
ID   I4DCC8_DESAJ            Unreviewed;       238 AA.
AC   I4DCC8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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   OrderedLocusNames=Desaci_4617 {ECO:0000313|EMBL:AFM43452.1};
OS   Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM43452.1, ECO:0000313|Proteomes:UP000002892};
RN   [1] {ECO:0000313|EMBL:AFM43452.1, ECO:0000313|Proteomes:UP000002892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22704 / JCM 16185 / SJ4
RC   {ECO:0000313|Proteomes:UP000002892};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
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; CP003639; AFM43452.1; -; Genomic_DNA.
DR   RefSeq; WP_014829432.1; NC_018068.1.
DR   AlphaFoldDB; I4DCC8; -.
DR   STRING; 646529.Desaci_4617; -.
DR   KEGG; dai:Desaci_4617; -.
DR   eggNOG; COG1922; Bacteria.
DR   HOGENOM; CLU_063203_3_1_9; -.
DR   OrthoDB; 9771846at2; -.
DR   UniPathway; UPA00632; -.
DR   Proteomes; UP000002892; 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:AFM43452.1};
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:AFM43452.1}.
SQ   SEQUENCE   238 AA;  26959 MW;  1E1130EAEE9E4143 CRC64;
     MRVNILGVTV DTYSMSETAE KIKLAVSAQR PIRVVTANPE IIYASQYNWA LKNVINSADI
     ITADGIGVVW AARQLGTQIE ERVTGIDLVQ SLFPIANAEK WRMYFLGGRP GIAEQAVKQV
     AEDYPGIVFH TSHGYFQPHE ESGILKEICE FRPDVLLVGL GAPRQEFWLA EHPGLTFVGI
     GVGGSFDALA GTVRRAPKQF QDLHIEWLYR LLKEPWRWKR QTVLPRFLFK VLWQRLKS
//
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