ID E5B0I6_ERWAM Unreviewed; 368 AA.
AC E5B0I6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
DE EC=2.7.8.33 {ECO:0000256|HAMAP-Rule:MF_02030};
DE AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
DE AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
GN Name=wecA {ECO:0000256|HAMAP-Rule:MF_02030,
GN ECO:0000313|EMBL:CBX78987.1};
GN ORFNames=EAIL5_0167 {ECO:0000313|EMBL:CBX78987.1};
OS Erwinia amylovora ATCC BAA-2158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX78987.1};
RN [1] {ECO:0000313|EMBL:CBX78987.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX78987.1};
RA Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT Restricted to Rubus Plants.";
RL J. Bacteriol. 193:785-786(2011).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_02030};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02030,
CC ECO:0000256|PIRSR:PIRSR600715-1};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02030};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02030}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02030}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02030}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02030}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02030}.
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DR EMBL; FR719183; CBX78987.1; -; Genomic_DNA.
DR AlphaFoldDB; E5B0I6; -.
DR UniPathway; UPA00281; -.
DR UniPathway; UPA00566; -.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06853; GT_WecA_like; 1.
DR HAMAP; MF_02030; WecA_Gammaproteo; 1.
DR InterPro; IPR012750; ECA_WecA-rel.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR NCBIfam; TIGR02380; ECA_wecA; 1.
DR PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR PANTHER; PTHR22926:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02030};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02030};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_02030};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW ECO:0000256|HAMAP-Rule:MF_02030};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02030, ECO:0000256|PIRSR:PIRSR600715-
KW 1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_02030};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02030};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02030};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02030};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02030}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 101..126
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 185..202
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 244..263
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 368 AA; 40949 MW; 386315E0FCC8D0A9 CRC64;
MNLLNTSTEL ALTFLFSLAF LFFARKAAKK IGLVDKPNYR KRHQGAIPLV GGISVFAGSC
FAFTLTDFYI PHIWLYSGCA GCLVMVGALD DRYDISVKFR AVVQAAVAVV MMMKAKIYLL
SLGYIFGPWE LIVGPFGYVL TLFAVWAAIN AFNMVDGIDG LLGGLSCVTF LAMGIILLFD
GQNSLAMWCF IMIAAIIPYI MLNLGMLGRR YKVFMGDAGS TLIGFTIIWI LLETTQGQNH
PITPVTALWL IAIPLMDMVA IMYRRLSKGM SPFSADRQHI HHLIMRAGFT SRQAFVLITA
AAALLALIGG LGEYLSFVPE WLMLVLFLLA FMLYGYCIKR AWRVARMIKR LKRRLRNSNN
ANKPSDDS
//
