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Database: UniProt
Entry: G5QS73_SALRU
LinkDB: G5QS73_SALRU
Original site: G5QS73_SALRU 
ID   G5QS73_SALRU            Unreviewed;       343 AA.
AC   G5QS73;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl {ECO:0000313|EMBL:EHC78629.1};
DE   Flags: Fragment;
GN   ORFNames=LTSERUB_6038 {ECO:0000313|EMBL:EHC78629.1};
OS   Salmonella enterica subsp. enterica serovar Rubislaw str. A4-653.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913081 {ECO:0000313|EMBL:EHC78629.1, ECO:0000313|Proteomes:UP000004903};
RN   [1] {ECO:0000313|EMBL:EHC78629.1, ECO:0000313|Proteomes:UP000004903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-653 {ECO:0000313|EMBL:EHC78629.1,
RC   ECO:0000313|Proteomes:UP000004903};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600715-1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EHC78629.1}.
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DR   EMBL; AFCT01002166; EHC78629.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5QS73; -.
DR   PATRIC; fig|913081.3.peg.4690; -.
DR   Proteomes; UP000004903; Unassembled WGS sequence.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR600715-1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHC78629.1"
SQ   SEQUENCE   343 AA;  38323 MW;  29B478838A4C6EE4 CRC64;
     RKVAKKIGLV DKPNFRKRHQ GLIPLVGGIS VYAGICFTFG IVDHYIPHAS LYLSCAGVLV
     LIGALDDRFD ISVKIRATIQ AAIGIIMMVF GKLYLSSLGY IFGSWEMVLG PFGYFLTLFA
     VWAAINAFNM VDGIDGLLGG LSSVSFAAMG LILWFDGQTS LAIWCFAMIA AILPYIMLNL
     GILGRRYKVF MGDAGSTLIG FTVIWILLET TQGKTHPISP VTALWIIAIP LMDMVAIMYR
     RLRKGMSPFS PDRQHIHHLI MRAGFTSRQA FVLITLAAAI LAGVGVAAEY SHFVPEWVML
     VLFLLAFFLY GYCIKRAWKV ARFIKRVKRR LRRHRKNRPN LTK
//
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