WECA_THEMA
ID WECA_THEMA Reviewed; 291 AA.
AC Q9X1N5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase;
DE EC=2.7.8.33;
DE AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase;
DE AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase;
GN Name=wecA; OrderedLocusNames=TM_1549;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION AS A TRANSFERASE, COFACTOR, ACTIVITY REGULATION, SUBSTRATE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18723618; DOI=10.1128/jb.00676-08;
RA Al-Dabbagh B., Mengin-Lecreulx D., Bouhss A.;
RT "Purification and characterization of the bacterial UDP-
RT GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA.";
RL J. Bacteriol. 190:7141-7146(2008).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=19442646; DOI=10.1016/j.ab.2009.05.011;
RA Al-Dabbagh B., Blanot D., Mengin-Lecreulx D., Bouhss A.;
RT "Preparative enzymatic synthesis of polyprenyl-pyrophosphoryl-
RT Nacetylglucosamine, an essential lipid intermediate for the biosynthesis of
RT various bacterial cell envelope polymers.";
RL Anal. Biochem. 391:163-165(2009).
CC -!- FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from
CC UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P),
CC yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55), the lipid
CC intermediate involved in the synthesis of various bacterial cell
CC envelope components. The enzyme is highly active when tested with C35-
CC P, instead of its natural C55-P lipid substrate, suggesting that at
CC least a 35-carbon chain is required for the lipid to be a substrate of
CC WecA. {ECO:0000269|PubMed:18723618}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-
CC undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:28090,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:60392,
CC ChEBI:CHEBI:62959; EC=2.7.8.33;
CC Evidence={ECO:0000269|PubMed:19442646};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18723618};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18723618};
CC -!- ACTIVITY REGULATION: Partially inhibited by magnesium at concentration
CC higher than 10 mM and totally inhibited at concentration higher than
CC 250 mM. Also inhibited by tunicamycin, NaCl and KCl.
CC {ECO:0000269|PubMed:18723618}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for C55-P (at pH 8 and at 65 degrees Celsius)
CC {ECO:0000269|PubMed:18723618};
CC KM=0.62 mM for UDP-GlcNAc (at pH 8 and at 65 degrees Celsius)
CC {ECO:0000269|PubMed:18723618};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:18723618};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. At 30 degrees Celsius
CC activity is only 7% of the optimal value and at 80 degrees Celsius,
CC the enzyme is totally inactive. {ECO:0000269|PubMed:18723618};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD36631.1; -; Genomic_DNA.
DR PIR; H72238; H72238.
DR RefSeq; NP_229349.1; NC_000853.1.
DR RefSeq; WP_004081942.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X1N5; -.
DR SMR; Q9X1N5; -.
DR STRING; 243274.THEMA_06535; -.
DR BindingDB; Q9X1N5; -.
DR ChEMBL; CHEMBL1932901; -.
DR PRIDE; Q9X1N5; -.
DR EnsemblBacteria; AAD36631; AAD36631; TM_1549.
DR KEGG; tma:TM1549; -.
DR eggNOG; COG0472; Bacteria.
DR InParanoid; Q9X1N5; -.
DR OMA; NIFEAHR; -.
DR OrthoDB; 728505at2; -.
DR BRENDA; 2.7.8.33; 6331.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
DR GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IDA:UniProtKB.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR PANTHER; PTHR22926; PTHR22926; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Magnesium; Manganese; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..291
FT /note="Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-
FT phosphate transferase"
FT /id="PRO_0000395353"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 72
FT /note="Important in orienting the substrate"
FT /evidence="ECO:0000250"
FT SITE 73
FT /note="Important in orienting the substrate; probably
FT interacts with magnesium or manganese"
FT /evidence="ECO:0000250"
FT SITE 128
FT /note="Could be required for catalysis"
FT /evidence="ECO:0000250"
FT SITE 131
FT /note="Could be required for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 291 AA; 32778 MW; 0B328CC164C9B85F CRC64;
MWEAIISFFL TSVLSVFAKK TEFLDRPDSR KSHGRAVPPV GGVSIFLTLL IFERDNPFFL
FSIPLFLLGL LDDLFDLSYR IKLAVTALVA VWFSTAVTIE VSIFGARIHP VFFVIWFVGM
VNAFNVVDGL DGLLSGISLF SSLMIGERSL AFSIIGFLPW NLPDAKVFLG NSGSFLLGAY
LSTASVVFFE GDLGYATLFL GFPFYEIVFS FVRRLVVKKN PFSPDEKHTH HVFSRKIGKW
KTLLILVSFS LMFNLLGLSQ KFYFIFLYVV LCCVLLFTYC VLQRGNGNLK L
