ID L8J8A9_9GAMM Unreviewed; 369 AA.
AC L8J8A9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=C942_03433 {ECO:0000313|EMBL:ELR63764.1};
OS Photobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR63764.1, ECO:0000313|Proteomes:UP000011134};
RN [1] {ECO:0000313|EMBL:ELR63764.1, ECO:0000313|Proteomes:UP000011134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK15 {ECO:0000313|EMBL:ELR63764.1,
RC ECO:0000313|Proteomes:UP000011134};
RA Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT "Genome Assembly of Photobacterium sp. AK15.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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:ELR63764.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMZO01000036; ELR63764.1; -; Genomic_DNA.
DR RefSeq; WP_007470156.1; NZ_AMZO01000036.1.
DR AlphaFoldDB; L8J8A9; -.
DR PATRIC; fig|1056511.3.peg.4357; -.
DR OrthoDB; 9783652at2; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000011134; 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..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 68..84
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 96..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 181..198
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 285..309
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 321..339
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 369 AA; 40412 MW; 4BDC13F203BF6E98 CRC64;
MSSAFLFVFI LSFCSLFIFR KVAKRIGLVD KPNARKLHQG VIPLVGGVSI FITLVITHLV
FSELTSDSLL FIVCATILVF TGVVDDRFDI SFKLRLLIQA GVSFAMMIIG GKSLHNLGYL
MGSEAIELSV AASYAITVLG VIGAINAFNM VDGIDGLLGG LASVTFGALG FMFFADGNMQ
LAMVCGVIVT AMVPYIMLNL GVPLGRRFKV FMGDAGSIFI GFTVIWLLIE ATQGTNTTHI
RPVTALWVIA IPLMDMATIM IRRIRKGQSP FKPDREHLHH ICQRIGLSSR MSLFVICMMA
SIMAGIGVWS DMAKINECVM FISFLSVFAV YFFVISYIWR ITTFIHRLFG VNKPTIPDAV
ASETSQSAE
//
