WECA_MYCLE
ID WECA_MYCLE Reviewed; 398 AA.
AC P45830;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Decaprenyl-phosphate N-acetylglucosaminephosphotransferase;
DE EC=2.7.8.35;
DE AltName: Full=Decaprenyl-phosphate GlcNAc-1-phosphate transferase;
DE AltName: Full=Decaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase;
DE AltName: Full=UDP-GlcNAc:decaprenyl-phosphate GlcNAc-1-phosphate transferase;
DE AltName: Full=UDP-N-acetylglucosamine--decaprenyl-phosphate N-acetylglucosaminephosphotransferase;
GN Name=wecA; Synonyms=rfe; OrderedLocusNames=ML1137;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Involved in the biosynthesis of the disaccharide D-N-
CC acetylglucosamine-L-rhamnose which plays an important role in the
CC mycobacterial cell wall as a linker connecting arabinogalactan and
CC peptidoglycan via a phosphodiester linkage. Catalyzes the transfer of
CC the N-acetylglucosamine-1-phosphate (GlcNAc-1P) moiety from UDP-GlcNAc
CC onto the carrier lipid decaprenyl phosphate (C50-P), yielding GlcNAc-
CC pyrophosphoryl-decaprenyl (GlcNAc-PP-C50) (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans,octa-cis-decaprenyl phosphate + UDP-N-acetyl-alpha-D-
CC glucosamine = N-acetyl-alpha-D-glucosaminyl-1-diphospho-trans,octa-
CC cis-decaprenol + UMP; Xref=Rhea:RHEA:34071, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:65079, ChEBI:CHEBI:65080; EC=2.7.8.35;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Mycobacteria use decaprenyl phosphate (C50-P) as a lipid
CC carrier in all known cell wall biosynthetic pathways, rather than the
CC usual undecaprenyl phosphate (C55-P) usually used in Gram-negative
CC bacteria. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC31518.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U15186; AAA63094.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31518.1; ALT_INIT; Genomic_DNA.
DR PIR; C87051; C87051.
DR PIR; T09982; T09982.
DR AlphaFoldDB; P45830; -.
DR SMR; P45830; -.
DR STRING; 272631.ML1137; -.
DR EnsemblBacteria; CAC31518; CAC31518; CAC31518.
DR KEGG; mle:ML1137; -.
DR Leproma; ML1137; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_2_2_11; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; ISS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; ISS:UniProtKB.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR PANTHER; PTHR22926; PTHR22926; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Magnesium; Manganese; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Decaprenyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /id="PRO_0000108950"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 126
FT /note="Important in orienting the substrate"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Important in orienting the substrate; probably
FT interacts with magnesium or manganese"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Could be required for catalysis"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Could be required for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 42089 MW; 37564293606CF9A6 CRC64;
MQYVREMSSD LATFASGLLA LFERSAGVPL RELALVGLTA AIITYFATGL VGVLANRLEA
VAYPRERDVH VTPTPRMGGL AMYLGVLAAV FLASQLPALT RGFVYSSGMP AVLVAGAVIT
GIGLIDDRWG LDALTKFAGQ ITAASVLVTM GVAWSVLYIP LGGVGTIVLD QTSSILLTLA
LTVSIVNAIN FVDGLDGLAA GLGLITAMAI CIFSVGLLRD HDGDVLFYPP AVISVVLAGS
CLGFLPHNFH RAKIFMGDSG SMLVGLMLAA ASTTAAGPIS QNAYGTRDVF ALLSPFLLVV
AVMFVPMLDL LLAIVRRIRA GRSAFSPDKM HLHHRLLQIG HSHRRVVLLI YLWVGIVAFG
AASTIFFNPR NTGAVMLGAI VITGMATVIP LLRRRDNY
