WECA_MYCS2
ID WECA_MYCS2 Reviewed; 406 AA.
AC A0R211;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
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; OrderedLocusNames=MSMEG_4947, MSMEI_4819;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=8631826; DOI=10.1074/jbc.271.13.7820;
RA Mikusova K., Mikus M., Besra G.S., Hancock I., Brennan P.J.;
RT "Biosynthesis of the linkaFge region of the mycobacterial cell wall.";
RL J. Biol. Chem. 271:7820-7828(1996).
RN [5]
RP LIPID CARRIER SPECIFICITY.
RX PubMed=15805521; DOI=10.1128/jb.187.8.2747-2757.2005;
RA Mahapatra S., Yagi T., Belisle J.T., Espinosa B.J., Hill P.J., McNeil M.R.,
RA Brennan P.J., Crick D.C.;
RT "Mycobacterial lipid II is composed of a complex mixture of modified
RT muramyl and peptide moieties linked to decaprenyl phosphate.";
RL J. Bacteriol. 187:2747-2757(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20637039; DOI=10.1111/j.1574-6968.2010.02045.x;
RA Jin Y., Xin Y., Zhang W., Ma Y.;
RT "Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947
RT have WecA function and MSMEG_4947 is required for the growth of M.
RT smegmatis.";
RL FEMS Microbiol. Lett. 310:54-61(2010).
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).
CC {ECO:0000269|PubMed:20637039}.
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 Evidence={ECO:0000269|PubMed:20637039};
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 -!- ACTIVITY REGULATION: Inhibited by tunicamycin.
CC {ECO:0000269|PubMed:8631826}.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8631826};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show drastic
CC morphological alterations before lysis and are unable to grow.
CC {ECO:0000269|PubMed:20637039}.
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:0000305|PubMed:15805521}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000480; ABK71461.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41264.1; -; Genomic_DNA.
DR RefSeq; WP_011730204.1; NZ_SIJM01000019.1.
DR RefSeq; YP_889199.1; NC_008596.1.
DR AlphaFoldDB; A0R211; -.
DR SMR; A0R211; -.
DR STRING; 246196.MSMEI_4819; -.
DR EnsemblBacteria; ABK71461; ABK71461; MSMEG_4947.
DR EnsemblBacteria; AFP41264; AFP41264; MSMEI_4819.
DR GeneID; 66736268; -.
DR KEGG; msg:MSMEI_4819; -.
DR KEGG; msm:MSMEG_4947; -.
DR PATRIC; fig|246196.19.peg.4826; -.
DR eggNOG; COG0472; Bacteria.
DR OMA; MCLGFLP; -.
DR OrthoDB; 728505at2; -.
DR BRENDA; 2.7.8.35; 3512.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Magnesium; Manganese; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..406
FT /note="Decaprenyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /id="PRO_0000420584"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 406 AA; 42390 MW; 7DC2897CDAC688CD CRC64;
MLQYGAPVIT ATRETGMDSQ VVLALSDTGA GVPLRELALV GLTAAIITYF ATGWVRVLAI
RFGAVAYPRE RDVHVQPTPR MGGLAMYIGV ASAVLLASQL PALTRGFVYS TGMPAVVVAG
GLIMAIGLID DRWGLDALTK FAGQITAASV LVTMGVAWSV LYIPIGGVGT IVLDQVSSIL
LTLALTVSII NAMNFVDGLD GLAAGLGLIT ALAICVFSVG LLRDHGGDVL FYPPAVISVV
LAGACLGFLP HNFHRAKIFM GDSGSMLIGL MLGAASTTAA GPISQNAYGA RDVFALLSPF
LLVVAVMLVP ALDTLLAIVR RTRAGRSPLS PDKMHLHHRL LQIGHSHRRA VLLIYLWVGI
IAFGAASTIF FDPGQTAMVM GVAIVVAIVV TLIPLLRRGP DGAQEP
