WECA_MYCTU
ID WECA_MYCTU Reviewed; 404 AA.
AC P9WMW5; L0T8Z6; Q10606;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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;
GN Name=wecA; Synonyms=rfe; OrderedLocusNames=Rv1302; ORFNames=MTCY373.22;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- 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}.
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DR EMBL; AL123456; CCP44059.1; -; Genomic_DNA.
DR PIR; B70774; B70774.
DR RefSeq; NP_215818.1; NC_000962.3.
DR RefSeq; WP_003898816.1; NZ_NVQJ01000030.1.
DR AlphaFoldDB; P9WMW5; -.
DR SMR; P9WMW5; -.
DR STRING; 83332.Rv1302; -.
DR PaxDb; P9WMW5; -.
DR DNASU; 886947; -.
DR GeneID; 45425276; -.
DR GeneID; 886947; -.
DR KEGG; mtu:Rv1302; -.
DR PATRIC; fig|83332.111.peg.1455; -.
DR TubercuList; Rv1302; -.
DR eggNOG; COG0472; Bacteria.
DR OMA; MCLGFLP; -.
DR PhylomeDB; P9WMW5; -.
DR BioCyc; MetaCyc:G185E-5476-MON; -.
DR BRENDA; 2.7.8.35; 3445.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; IDA:MTBBASE.
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 GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IBA:GO_Central.
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..404
FT /note="Decaprenyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /id="PRO_0000108951"
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 259..279
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 404 AA; 42257 MW; 57D7D2807034A426 CRC64;
MQYGLEVSSD VAGVAGGLLA LSYRGAGVPL RELALVGLTA AIITYFATGP VRMLASRLGA
VAYPRERDVH VTPTPRMGGL AMFLGIVGAV FLASQLPALT RGFVYSTGMP AVLVAGAVIM
GIGLIDDRWG LDALTKFAGQ ITAASVLVTM GVAWSVLYIP VGGVGTIVLD QASSILLTLA
LTVSIVNAMN FVDGLDGLAA GLGLITALAI CMFSVGLLRD HGGDVLYYPP AVISVVLAGA
CLGFLPHNFH RAKIFMGDSG SMLIGLMLAA ASTTAAGPIS QNAYGARDVF ALLSPFLLVV
AVMFVPMLDL LLAIVRRTRA GRSAFSPDKM HLHHRLLQIG HSHRRVVLII YLWVGIVAFG
AASSIFFNPR DTAAVMLGAI VVAGVATLIP LLRRGDDYYD PDLD
