ID A7MQH9_CROS8 Unreviewed; 366 AA.
AC A7MQH9;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
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 OrderedLocusNames=ESA_03774 {ECO:0000313|EMBL:ABU78966.1};
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU78966.1, ECO:0000313|Proteomes:UP000000260};
RN [1] {ECO:0000313|EMBL:ABU78966.1, ECO:0000313|Proteomes:UP000000260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU78966.1,
RC ECO:0000313|Proteomes:UP000000260};
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU78966.1; -; Genomic_DNA.
DR RefSeq; WP_012126056.1; NC_009778.1.
DR AlphaFoldDB; A7MQH9; -.
DR GeneID; 56732425; -.
DR KEGG; esa:ESA_03774; -.
DR HOGENOM; CLU_023982_1_0_6; -.
DR UniPathway; UPA00281; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000000260; 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:UP000000260};
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..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 72..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 101..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 131..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..316
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 322..343
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 366 AA; 40721 MW; E8FE21A91EDBA633 CRC64;
MNLVTVGTEL LSIFLFTFVF LFFARKIGKR VGLVDKPNFR KRHQGLIPLV GGISVYAGIC
FTFFIADYYI PHAALYLASA GVLVFVGALD DRYDISVKIR AVIQAVIGVV MMTVGGLYLR
SLGYIFGSWE MVLGPFGYFL TLFAVWAAIN AFNMVDGIDG LLGGLSCVSF AAIGMILWFD
GQTSLSMWCF AMIAAILPYI LLNLGAFGRR YKVFMGDAGS TLIGFTVIWI LLETTQGKTH
PISPVTALWI IAIPLMDMIA IMYRRLRKGM SPFSPDRQHI HHLIMRAGFT SRQAFVLITL
AAALLAGIGV ASEYAAHIIP EWVMLALFLL AFFFYGYCIK RAWKVARFIK RVKRRIKRGS
NKPTAN
//
