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Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase (EC 2.7.8.33) (UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase) (Undecaprenyl-phosphate GlcNAc-1-phosphate transferase)

 WECA_THEMA              Reviewed;         291 AA.
Q9X1N5;
13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
07-JUN-2017, entry version 94.
RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase;
EC=2.7.8.33;
AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase;
AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase;
Name=wecA; OrderedLocusNames=TM_1549;
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
NCBI_TaxID=243274;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
PubMed=10360571; DOI=10.1038/20601;
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Evidence for lateral gene transfer between Archaea and Bacteria from
genome sequence of Thermotoga maritima.";
Nature 399:323-329(1999).
[2]
FUNCTION AS A TRANSFERASE, COFACTOR, ENZYME REGULATION, SUBSTRATE
SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18723618; DOI=10.1128/JB.00676-08;
Al-Dabbagh B., Mengin-Lecreulx D., Bouhss A.;
"Purification and characterization of the bacterial UDP-
GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA.";
J. Bacteriol. 190:7141-7146(2008).
[3]
CATALYTIC ACTIVITY.
PubMed=19442646; DOI=10.1016/j.ab.2009.05.011;
Al-Dabbagh B., Blanot D., Mengin-Lecreulx D., Bouhss A.;
"Preparative enzymatic synthesis of polyprenyl-pyrophosphoryl-
Nacetylglucosamine, an essential lipid intermediate for the
biosynthesis of various bacterial cell envelope polymers.";
Anal. Biochem. 391:163-165(2009).
-!- FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety
from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate
(C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-
C55), the lipid intermediate involved in the synthesis of various
bacterial cell envelope components. The enzyme is highly active
when tested with C35-P, instead of its natural C55-P lipid
substrate, suggesting that at least a 35-carbon chain is required
for the lipid to be a substrate of WecA.
{ECO:0000269|PubMed:18723618}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine +
ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-
glucosaminyl-diphospho-ditrans,octacis-undecaprenol.
{ECO:0000269|PubMed:19442646}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:18723618};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:18723618};
-!- ENZYME REGULATION: Partially inhibited by magnesium at
concentration higher than 10 mM and totally inhibited at
concentration higher than 250 mM. Also inhibited by tunicamycin,
NaCl and KCl. {ECO:0000269|PubMed:18723618}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.12 mM for C55-P (at pH 8 and at 65 degrees Celsius)
{ECO:0000269|PubMed:18723618};
KM=0.62 mM for UDP-GlcNAc (at pH 8 and at 65 degrees Celsius)
{ECO:0000269|PubMed:18723618};
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:18723618};
Temperature dependence:
Optimum temperature is 65 degrees Celsius. At 30 degrees Celsius
activity is only 7% of the optimal value and at 80 degrees
Celsius, the enzyme is totally inactive.
{ECO:0000269|PubMed:18723618};
-!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide
biosynthesis.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
subfamily. {ECO:0000305}.
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EMBL; AE000512; AAD36631.1; -; Genomic_DNA.
PIR; H72238; H72238.
RefSeq; NP_229349.1; NC_000853.1.
RefSeq; WP_004081942.1; NZ_CP011107.1.
STRING; 243274.TM1549; -.
BindingDB; Q9X1N5; -.
ChEMBL; CHEMBL1932901; -.
EnsemblBacteria; AAD36631; AAD36631; TM_1549.
GeneID; 897567; -.
KEGG; tma:TM1549; -.
eggNOG; ENOG4107UKG; Bacteria.
eggNOG; COG0472; LUCA.
InParanoid; Q9X1N5; -.
KO; K02851; -.
OMA; WRITAFL; -.
BRENDA; 2.7.8.33; 6331.
UniPathway; UPA00963; -.
Proteomes; UP000008183; Chromosome.
GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IDA:UniProtKB.
GO; GO:0071555; P:cell wall organization; IDA:UniProtKB.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
InterPro; IPR000715; Glycosyl_transferase_4.
PANTHER; PTHR22926; PTHR22926; 1.
Pfam; PF00953; Glycos_transf_4; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Glycosyltransferase; Magnesium;
Manganese; Membrane; Reference proteome; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 291 Undecaprenyl-phosphate alpha-N-
acetylglucosaminyl 1-phosphate
transferase.
/FTId=PRO_0000395353.
TRANSMEM 4 24 Helical. {ECO:0000255}.
TRANSMEM 32 52 Helical. {ECO:0000255}.
TRANSMEM 57 77 Helical. {ECO:0000255}.
TRANSMEM 84 104 Helical. {ECO:0000255}.
TRANSMEM 110 130 Helical. {ECO:0000255}.
TRANSMEM 138 160 Helical. {ECO:0000255}.
TRANSMEM 167 189 Helical. {ECO:0000255}.
TRANSMEM 194 216 Helical. {ECO:0000255}.
TRANSMEM 237 257 Helical. {ECO:0000255}.
TRANSMEM 262 282 Helical. {ECO:0000255}.
SITE 72 72 Important in orienting the substrate.
{ECO:0000250}.
SITE 73 73 Important in orienting the substrate;
probably interacts with magnesium or
manganese. {ECO:0000250}.
SITE 128 128 Could be required for catalysis.
{ECO:0000250}.
SITE 131 131 Could be required for catalysis.
{ECO:0000250}.
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


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