LST_NEIGO
ID LST_NEIGO Reviewed; 371 AA.
AC P72074;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase {ECO:0000305|PubMed:8910446};
DE EC=2.4.99.6 {ECO:0000250|UniProtKB:P72097};
DE AltName: Full=CMP-N-acetylneuraminate:beta-galactoside alpha-2,3-sialyltransferase {ECO:0000303|PubMed:8910446};
DE Short=CMP-Neu5Ac:beta-galactoside alpha-2,3-sialyltransferase {ECO:0000303|PubMed:8910446};
DE AltName: Full=Lipooligosaccharide sialyltransferase {ECO:0000303|PubMed:12065517, ECO:0000303|PubMed:8910446};
DE Short=LOS sialyltransferase {ECO:0000303|PubMed:12065517, ECO:0000303|PubMed:8910446};
GN Name=lst {ECO:0000303|PubMed:8910446};
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33084 / F62 / M-1914;
RX PubMed=8910446; DOI=10.1074/jbc.271.45.28271;
RA Gilbert M., Watson D.C., Cunningham A.-M., Jennings M.P., Young N.M.,
RA Wakarchuk W.W.;
RT "Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the
RT bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae.";
RL J. Biol. Chem. 271:28271-28276(1996).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 33084 / F62 / M-1914;
RX PubMed=12065517; DOI=10.1128/iai.70.7.3744-3751.2002;
RA Shell D.M., Chiles L., Judd R.C., Seal S., Rest R.F.;
RT "The Neisseria lipooligosaccharide-specific alpha-2,3-sialyltransferase is
RT a surface-exposed outer membrane protein.";
RL Infect. Immun. 70:3744-3751(2002).
RN [3]
RP FUNCTION, ROLE IN VIRULENCE, AND PATHWAY.
RC STRAIN=ATCC 33084 / F62 / M-1914;
RX PubMed=25650401; DOI=10.1128/mbio.02465-14;
RA Lewis L.A., Gulati S., Burrowes E., Zheng B., Ram S., Rice P.A.;
RT "alpha-2,3-sialyltransferase expression level impacts the kinetics of
RT lipooligosaccharide sialylation, complement resistance, and the ability of
RT Neisseria gonorrhoeae to colonize the murine genital tract.";
RL MBio 6:E02465-E02465(2015).
CC -!- FUNCTION: Catalyzes the transfer of sialic acid from the substrate CMP-
CC N-acetylneuraminate to the terminal galactose residue of the lacto-N-
CC neotetraose branch of surface lipooligosaccharide (LOS), forming an
CC alpha-2,3-sialyl linkage. Thus, functions in the sialylation of LOS,
CC which plays a role in the evasion of the host immune response by
CC protecting N.gonorrhoeae from complement-mediated serum killing and
CC from phagocytic killing by neutrophils, and which is critical for
CC establishing infection. {ECO:0000269|PubMed:12065517,
CC ECO:0000269|PubMed:25650401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:52316,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:136545; EC=2.4.99.6;
CC Evidence={ECO:0000250|UniProtKB:P72097};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipooligosaccharide
CC biosynthesis. {ECO:0000269|PubMed:12065517,
CC ECO:0000269|PubMed:25650401}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P72097}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:12065517}; Peripheral membrane protein
CC {ECO:0000305}; Extracellular side {ECO:0000269|PubMed:12065517}.
CC Note=Is exclusively found in outer membrane preparations of the
CC pathogen and is surface exposed. Inner membrane, periplasmic,
CC cytoplasmic, and culture supernatant fractions are devoid of Lst.
CC {ECO:0000269|PubMed:12065517}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not express
CC sialyltransferase activity onto LOS. {ECO:0000269|PubMed:12065517}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 52 family.
CC {ECO:0000305}.
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DR EMBL; U60664; AAC44539.1; -; Genomic_DNA.
DR AlphaFoldDB; P72074; -.
DR SMR; P72074; -.
DR CAZy; GT52; Glycosyltransferase Family 52.
DR UniPathway; UPA00501; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR012477; Glyco_transf_52.
DR Pfam; PF07922; Glyco_transf_52; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Glycosyltransferase; Lipopolysaccharide biosynthesis;
KW Membrane; Transferase; Virulence.
FT CHAIN 1..371
FT /note="N-acetyllactosaminide alpha-2,3-sialyltransferase"
FT /id="PRO_0000080572"
FT ACT_SITE 258
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT ACT_SITE 280
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT BINDING 255
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT BINDING 278..282
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT BINDING 299..300
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT BINDING 322..323
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:P72097"
SQ SEQUENCE 371 AA; 42682 MW; C197AD342E87F461 CRC64;
MGLKKVCLTV LCLIVFCFGI FYTFDRVNQG ERNAVSLLKD KLFNEEGKPV NLIFCYTILQ
MKVAERIMAQ HPGERFYVVL MSENRNEKYD YYFNQIKDKA ERAYFFYLPY GLNKSFNFIP
TMAELKVKSM LLPKVKRIYL ASLEKVSIAA FLSTYPDAEI KTFDDGTNNL IRESSYLGGE
FAVNGAIKRN FARMMVGDWS IAKTRNASDE HYTIFKGLKN IMDDGRRKMT YLPLFDASEL
KAGDETGGTV RILLGSPDKE MKEISEKAAK NFNIQYVAPH PRQTYGLSGV TALNSPYVIE
DYILREIKKN PHTRYEIYTF FSGAALTMKD FPNVHVYALK PASLPEDYWL KPVYALFRQA
DIPILTFDDK N
