ID A4XJ66_CALS8 Unreviewed; 612 AA.
AC A4XJ66;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=Csac_1349 {ECO:0000313|EMBL:ABP66951.1};
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS 6331).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP66951.1, ECO:0000313|Proteomes:UP000000256};
RN [1] {ECO:0000313|Proteomes:UP000000256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC {ECO:0000313|Proteomes:UP000000256};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA Kengen S.M.W., Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP66951.1, ECO:0000313|Proteomes:UP000000256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC {ECO:0000313|Proteomes:UP000000256};
RX PubMed=18776029; DOI=10.1128/AEM.00968-08;
RA van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K.,
RA Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E.,
RA van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J.,
RA Kelly R.M., Kengen S.W.;
RT "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor
RT saccharolyticus.";
RL Appl. Environ. Microbiol. 74:6720-6729(2008).
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; CP000679; ABP66951.1; -; Genomic_DNA.
DR RefSeq; WP_011916887.1; NC_009437.1.
DR AlphaFoldDB; A4XJ66; -.
DR STRING; 351627.Csac_1349; -.
DR CAZy; GT26; Glycosyltransferase Family 26.
DR KEGG; csc:Csac_1349; -.
DR eggNOG; COG1922; Bacteria.
DR eggNOG; COG2327; Bacteria.
DR HOGENOM; CLU_445979_0_0_9; -.
DR OrthoDB; 3199616at2; -.
DR UniPathway; UPA00632; -.
DR Proteomes; UP000000256; 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR HAMAP; MF_02070; TagA_TarA; 1.
DR InterPro; IPR007345; Polysacch_pyruvyl_Trfase.
DR InterPro; IPR019896; Polysacch_pyruvyl_Trfase_CsaB.
DR InterPro; IPR034714; TagA_TarA.
DR InterPro; IPR004629; WecG_TagA_CpsF.
DR NCBIfam; TIGR03609; S_layer_CsaB; 1.
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.
DR Pfam; PF04230; PS_pyruv_trans; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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:ABP66951.1};
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:ABP66951.1}.
FT DOMAIN 14..299
FT /note="Polysaccharide pyruvyl transferase"
FT /evidence="ECO:0000259|Pfam:PF04230"
SQ SEQUENCE 612 AA; 70468 MW; 97C845567E488DF9 CRC64;
MKNIVISGYY GQLNTGDEAI LRVLVDRLKE YERESNSSLN IVVLSSRPEL TARLYNVESV
NRKKIPSVIK AIKRCDIFIS GGGSLFQNET SNRSLYYYLF QILVAKLFGK KVFIFSQGIG
PIKRWYNILL FKHVIKLADY ITVRDYDSFD FLHKLKINKE VELSADPAFL LNPCCDQKIQ
KLLEEYDIDF SKKTVGIVVR KWKKEKNMTD KIAEIADILI ENEGYNVIFI PFQGKWDIIK
INEIVSKMKN RPYVLSEKLS AHELLGIFKK LDLVVGMRLH ALVFAAKMGV KFIGISYDPK
IDSFLKIYGF KPAGYVDSFD ENNVLISVQY MLSDGKVTKK IDEITKNMTQ KAEKAFEILR
EALNNIKKKD SINILGVRID CVNFKKAKEK CLEFLNSSSP HIVFTPNVEM IMLAQKDEKF
KKILNSSDLN VPDGIGVVWA SKYFGEKLYE RVTGFDLMME LMPELERHQK RVFLLGAKPS
VAEKAKENLL KIFKNLSICG THHGYFSQEE NEKVIELINS SKADVVFVAM GMKKQEEWIY
KNKKKLNCKL IMGVGGSLDV LSGEVKRAPK IFQKLGLEWF YRLITQPWRF KRMLALPKFI
FVVLKTKLFG GR
//
