ID Q814L0_BACCR Unreviewed; 246 AA.
AC Q814L0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 98.
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=BC_5419 {ECO:0000313|EMBL:AAP12281.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP12281.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP12281.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP12281.1; -; Genomic_DNA.
DR RefSeq; NP_835080.1; NC_004722.1.
DR RefSeq; WP_000290748.1; NZ_CP034551.1.
DR AlphaFoldDB; Q814L0; -.
DR CAZy; GT26; Glycosyltransferase Family 26.
DR KEGG; bce:BC5419; -.
DR PATRIC; fig|226900.8.peg.5598; -.
DR HOGENOM; CLU_063203_3_1_9; -.
DR OrthoDB; 9771846at2; -.
DR UniPathway; UPA00632; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
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:AAP12281.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417};
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:AAP12281.1}.
SQ SEQUENCE 246 AA; 27679 MW; 91BA454DF104485B CRC64;
MAVQTVDILG VPFSTMTMDE TVQYLKEQLE AERTHTFQVV TANPEIVMCA KKDEKFYQTL
LNTDLITPDG IGVVKASGML GTPLKERVAG FDLMCNLLAK LSEDSKPVSV FLLGAKPHVV
QAAADHLTKT YSAVSIAGIQ DGYFKQEDEE NIISRIQEAK PDLLLVALGF PRQENFIQNN
KHRLETKMAV GVGGSLDVWA GEVKRAPKWI QAIHLEWFYR LCSNPTRWRR QLVLAEFLKE
VMRSKK
//
