WECA_PASMU
ID WECA_PASMU Reviewed; 357 AA.
AC Q9CNG8;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030};
DE EC=2.7.8.33 {ECO:0000255|HAMAP-Rule:MF_02030};
DE AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030};
DE AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030};
GN Name=wecA {ECO:0000255|HAMAP-Rule:MF_02030}; Synonyms=rfe;
GN OrderedLocusNames=PM0463;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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).
CC {ECO:0000255|HAMAP-Rule:MF_02030}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02030};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02030};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02030};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02030}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02030}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02030}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02030}.
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DR EMBL; AE004439; AAK02547.1; -; Genomic_DNA.
DR RefSeq; WP_005751351.1; NC_002663.1.
DR AlphaFoldDB; Q9CNG8; -.
DR SMR; Q9CNG8; -.
DR STRING; 747.DR93_1235; -.
DR EnsemblBacteria; AAK02547; AAK02547; PM0463.
DR GeneID; 62226740; -.
DR KEGG; pmu:PM0463; -.
DR HOGENOM; CLU_023982_1_0_6; -.
DR OMA; MCLGFLP; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-UniRule.
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; ISS:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02030; WecA_Gammaproteo; 1.
DR InterPro; IPR012750; ECA_WecA-rel.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR PANTHER; PTHR22926; PTHR22926; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
DR TIGRFAMs; TIGR02380; ECA_wecA; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipopolysaccharide biosynthesis; Magnesium; Manganese; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..357
FT /note="Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-
FT phosphate transferase"
FT /id="PRO_0000108949"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02030"
SQ SEQUENCE 357 AA; 40286 MW; B82A186EA21EED5C CRC64;
MLLSLIVTFL GAFLTLLFMR PIAQKIGLVD KPNFRKRHQG AIPLIGGVSL FVGNLCFYLL
EWEQMRLPTL YLFSIFVLLV IGMIDDRFDI SPFLRAGIQA ILAILMIDLG NLYLDHLGQI
LGPFQLTLGS IGLIITVLAT IAAINAFNMI DGIDGLLGGL SSVAFVSIGI LLIKDNQLDL
AYWSFALIIA ILPYFMMNLG IPFGQKFKVF MGDAGSTLIG FTIIWILLLS TQGKGHPMNP
VTALWIIAIP LIDMIAIMYR RLRKGKSPFR PDRLHVHHLM MRAGLTSRQA FLLITFAAAI
CATIGILGEI FYINEWLMFA GFILLFFMYS YSITRAWRIT RWIRRMRRRA KRIHNKG
