ID D2YB46_VIBMI Unreviewed; 366 AA.
AC D2YB46;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 ORFNames=VMB_07430 {ECO:0000313|EMBL:EEW08000.1};
OS Vibrio mimicus VM603.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=671074 {ECO:0000313|EMBL:EEW08000.1, ECO:0000313|Proteomes:UP000004827};
RN [1] {ECO:0000313|EMBL:EEW08000.1, ECO:0000313|Proteomes:UP000004827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM603 {ECO:0000313|EMBL:EEW08000.1,
RC ECO:0000313|Proteomes:UP000004827};
RX PubMed=19860885; DOI=10.1186/1471-2148-9-258;
RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T.,
RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.;
RT "Genomic taxonomy of Vibrios.";
RL BMC Evol. Biol. 9:258-258(2009).
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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEW08000.1}.
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DR EMBL; ACYU01000023; EEW08000.1; -; Genomic_DNA.
DR RefSeq; WP_000586524.1; NZ_ACYU01000023.1.
DR AlphaFoldDB; D2YB46; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000004827; Unassembled WGS sequence.
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: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..22
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 133..151
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 183..200
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 286..314
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 366 AA; 40372 MW; E3FD73D5BB428887 CRC64;
MIIPFIDLGF LFFFSLTSLF VLRKVAKKIG LVDKPNERKL HQGAIPLVGG IAICFSLAYF
LFNNPSVIPH SPLYATCITL LVIVGALDDK YDLNFKIRII IQAGLSIAMM MIGGIELHTI
GNVFGFGEVK LGLTGYVITI LAVVGSINAF NMVDGIDGLL GALSIVTFGG LGLMLAYDGQ
PQLAYLCLVM IVIILPYILL NIGAFGRKRK VFMGDAGSML IGFTVIWFLL LSSQNGKTPP
LRPITALWLI AVPLMDMAAI MLRRIRRGDS PFKPDREHLH HIFQRLGLSS LQTVLAISLI
AASFAACGIL GEIYNLREAF MFYSFIACFA IYAMLLNYVW RVTRFVRTLL GIKDTPQEIK
HGMDKS
//
