ID   WAAK_SALTY              Reviewed;         381 AA.
AC   P26470;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Lipopolysaccharide 1,2-N-acetylglucosaminetransferase {ECO:0000305};
DE            EC=2.4.1.56 {ECO:0000269|PubMed:24479701};
GN   Name=waaK {ECO:0000303|PubMed:24479701};
GN   Synonyms=rfaK {ECO:0000303|PubMed:1657881}; OrderedLocusNames=STM3714;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=1657881; DOI=10.1128/jb.173.22.7151-7163.1991;
RA   Maclachlan P.R., Kadam S.K., Sanderson K.E.;
RT   "Cloning, characterization, and DNA sequence of the rfaLK region for
RT   lipopolysaccharide synthesis in Salmonella typhimurium LT2.";
RL   J. Bacteriol. 173:7151-7163(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=Ty2;
RX   PubMed=16495526; DOI=10.1128/iai.74.3.1555-1564.2006;
RA   Hoare A., Bittner M., Carter J., Alvarez S., Zaldivar M., Bravo D.,
RA   Valvano M.A., Contreras I.;
RT   "The outer core lipopolysaccharide of Salmonella enterica serovar Typhi is
RT   required for bacterial entry into epithelial cells.";
RL   Infect. Immun. 74:1555-1564(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=LT2;
RX   PubMed=24479701; DOI=10.1021/bi4015665;
RA   Qian J., Garrett T.A., Raetz C.R.;
RT   "In vitro assembly of the outer core of the lipopolysaccharide from
RT   Escherichia coli K-12 and Salmonella typhimurium.";
RL   Biochemistry 53:1250-1262(2014).
CC   -!- FUNCTION: Transferase involved in the biosynthesis of the core
CC       oligosaccharide region of lipopolysaccharide (LPS) (PubMed:24479701).
CC       Catalyzes the addition of the terminal N-acetyl-D-glucosamine (GlcNAc)
CC       group to the outer-core glucose II, the last step of the lipid A-core
CC       oligosaccharide biosynthesis (PubMed:24479701).
CC       {ECO:0000269|PubMed:24479701}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-N-acetyl-alpha-D-glucosamine + [lipopolysaccharide] = UDP
CC         + N-acetyl-alpha-D-glucosaminyl-[lipopolysaccharide].; EC=2.4.1.56;
CC         Evidence={ECO:0000269|PubMed:24479701};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000269|PubMed:24479701, ECO:0000305|PubMed:1657881}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:1657881};
CC       Peripheral membrane protein {ECO:0000305|PubMed:1657881}.
CC   -!- DISRUPTION PHENOTYPE: Mutant lacks a terminal outer core GlcNAc residue
CC       and does not express the O antigen, but it can invade epithelial cells
CC       as efficiently as the wild-type strain. {ECO:0000269|PubMed:16495526}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; M73826; AAA27207.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22573.1; -; Genomic_DNA.
DR   PIR; C41317; C41317.
DR   RefSeq; NP_462614.1; NC_003197.2.
DR   RefSeq; WP_000591818.1; NC_003197.2.
DR   AlphaFoldDB; P26470; -.
DR   SMR; P26470; -.
DR   STRING; 99287.STM3714; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PaxDb; 99287-STM3714; -.
DR   DNASU; 1255238; -.
DR   GeneID; 1255238; -.
DR   KEGG; stm:STM3714; -.
DR   PATRIC; fig|99287.12.peg.3928; -.
DR   HOGENOM; CLU_009583_38_1_6; -.
DR   OMA; SVHNEMF; -.
DR   PhylomeDB; P26470; -.
DR   BioCyc; MetaCyc:STM3714-MONOMER; -.
DR   BioCyc; SENT99287:STM3714-MONOMER; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008917; F:lipopolysaccharide N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03801; GT4_PimA-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR45947; SULFOQUINOVOSYL TRANSFERASE SQD2; 1.
DR   PANTHER; PTHR45947:SF3; SULFOQUINOVOSYL TRANSFERASE SQD2; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Glycosyltransferase;
KW   Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase.
FT   CHAIN           1..381
FT                   /note="Lipopolysaccharide 1,2-N-
FT                   acetylglucosaminetransferase"
FT                   /id="PRO_0000080306"
SQ   SEQUENCE   381 AA;  43152 MW;  F60F37FF175372C6 CRC64;
     MIKKIIFTVT PIFSIPPRGA AAVETWIYQV AKRLSIPNAI ACIKNAGYPE YNKINDNCDI
     HYIGFSKVYK RLFQKWTRLD PLPYSQRILN IRDKVTTQED SVIVIHNSMK LYRQIRERNP
     NAKLVMHMHN AFEPELPDND AKIIVPSQFL KAFYEERLPA AAVSIVPNGF CAETYKRNPQ
     DNLRQQLNIA EDATVLLYAG RISPDKGILL LLQAFKQLRT LRSNIKLVVV GDPYASRKGE
     KAEYQKKVLD AAKEIGTDCI MAGGQSPDQM HNFYHIADLV IVPSQVEEAF CMVAVEAMAA
     GKAVLASKKG GISEFVLDGI TGYHLAEPMS SDSIINDINR ALADKERHQI AEKAKSLVFS
     KYSWENVAQR FEEQMKNWFD K
//