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Database: UniProt
Entry: A0A0M2KC70_9GAMM
LinkDB: A0A0M2KC70_9GAMM
Original site: A0A0M2KC70_9GAMM 
ID   A0A0M2KC70_9GAMM        Unreviewed;       359 AA.
AC   A0A0M2KC70;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=AV903_20375 {ECO:0000313|EMBL:AXF77850.1}, SY86_15610
GN   {ECO:0000313|EMBL:KKF36539.1};
OS   Erwinia tracheiphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF36539.1, ECO:0000313|Proteomes:UP000033924};
RN   [1] {ECO:0000313|EMBL:KKF36539.1, ECO:0000313|Proteomes:UP000033924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BuffGH {ECO:0000313|EMBL:KKF36539.1,
RC   ECO:0000313|Proteomes:UP000033924};
RA   Shapiro L.R.;
RT   "Erwinia tracheiphila.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AXF77850.1, ECO:0000313|Proteomes:UP000264980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDcuke {ECO:0000313|EMBL:AXF77850.1,
RC   ECO:0000313|Proteomes:UP000264980};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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   -!- 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; CP013970; AXF77850.1; -; Genomic_DNA.
DR   EMBL; JXNU01000003; KKF36539.1; -; Genomic_DNA.
DR   RefSeq; WP_040465773.1; NZ_JXNU01000003.1.
DR   AlphaFoldDB; A0A0M2KC70; -.
DR   STRING; 65700.SY86_15610; -.
DR   PATRIC; fig|65700.7.peg.3905; -.
DR   UniPathway; UPA00281; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000033924; Unassembled WGS sequence.
DR   Proteomes; UP000264980; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000033924};
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..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        70..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..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        324..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   359 AA;  39865 MW;  08BBD1E0444EE36C CRC64;
     MNLLNMSTEL ALIFLFSLVF LFFARKVAKR IGLVDKPNYR KRHQGVIPLV GGISVFAGIC
     FGFIITNYYI PHFLLYLSCA GVLVLVGALD DRFDISVKIR AFVQAAIAVV MMSVGKLYLL
     SLGYIFGPWE LVVGPFGYVL TLFAVWAAIN AFNMVDGIDG LLGGLSCVTF LAMGIILLLG
     GQQSLAMWCF AMIAAIVPYI LLNLGAFGGR YKVFMGDAGS TLIGFTIIWI LLEATQGQYH
     PITPVTALWL IAIPLMDMVA IMYRRLSKGM SPFSADRQHI HHLIMRAGFT SKQACFLITL
     AAALLAGIGV LCESLSFVPE WLMLAFYLVA FMLYGYCIKR AWRVARLIKR VKRRLRRVN
//
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