ID D9TSU1_THETC Unreviewed; 243 AA.
AC D9TSU1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=Tthe_0543 {ECO:0000313|EMBL:ADL68106.1};
OS Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS thermosaccharolyticum).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=580327 {ECO:0000313|EMBL:ADL68106.1, ECO:0000313|Proteomes:UP000001626};
RN [1] {ECO:0000313|EMBL:ADL68106.1, ECO:0000313|Proteomes:UP000001626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC 00135 / 2032 {ECO:0000313|Proteomes:UP000001626};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT 571.";
RL Submitted (AUG-2010) 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; CP002171; ADL68106.1; -; Genomic_DNA.
DR RefSeq; WP_013297081.1; NC_014410.1.
DR AlphaFoldDB; D9TSU1; -.
DR STRING; 580327.Tthe_0543; -.
DR CAZy; GT26; Glycosyltransferase Family 26.
DR KEGG; ttm:Tthe_0543; -.
DR eggNOG; COG1922; Bacteria.
DR HOGENOM; CLU_063203_3_1_9; -.
DR OrthoDB; 9771846at2; -.
DR UniPathway; UPA00632; -.
DR Proteomes; UP000001626; 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:ADL68106.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001626};
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:ADL68106.1}.
SQ SEQUENCE 243 AA; 27879 MW; A78A59AF24299408 CRC64;
MADRFVIFGV PIDKVTMKKA VDIVENFLLE DRLHIVATPN AEIVMMAQND DEYKEILNKT
DLNVPDGSGV IFASKIYKEE LPERVAGFDL MMELIKIASL KHYKIYLLGA KADVVKGAYL
NLKSRYQGID IVGFHDGYFS EIDEEEIIND INEKKTDLLF VALGAPKQEK WIYKNRNKLN
AKVAIGVGGS FDVIAGKVTR APEIYRKLGL EWFYRLMKEP WRYKRMMALP RFAMKVLFSK
KSV
//
