LST_NEIMA
ID LST_NEIMA Reviewed; 371 AA.
AC Q9JUV5; A1IRE0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase {ECO:0000250|UniProtKB:P72097};
DE EC=2.4.99.6 {ECO:0000250|UniProtKB:P72097};
DE AltName: Full=CMP-N-acetylneuraminate:beta-galactoside alpha-2,3-sialyltransferase {ECO:0000250|UniProtKB:P72097};
DE Short=CMP-Neu5Ac:beta-galactoside alpha-2,3-sialyltransferase {ECO:0000250|UniProtKB:P72097};
DE AltName: Full=Lipooligosaccharide sialyltransferase {ECO:0000250|UniProtKB:P72097};
DE Short=LOS sialyltransferase {ECO:0000250|UniProtKB:P72097};
GN Name=lst {ECO:0000250|UniProtKB:P72097}; OrderedLocusNames=NMA1118;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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.meningitidis from complement-mediated serum killing and
CC from phagocytic killing by neutrophils. {ECO:0000250|UniProtKB:P72097}.
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:0000250|UniProtKB:P72097}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P72097}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P72097}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P72097}; Extracellular side
CC {ECO:0000250|UniProtKB:P72097}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 52 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL157959; CAM08326.1; -; Genomic_DNA.
DR PIR; B81878; B81878.
DR RefSeq; WP_002236898.1; NC_003116.1.
DR AlphaFoldDB; Q9JUV5; -.
DR SMR; Q9JUV5; -.
DR CAZy; GT52; Glycosyltransferase Family 52.
DR EnsemblBacteria; CAM08326; CAM08326; NMA1118.
DR KEGG; nma:NMA1118; -.
DR HOGENOM; CLU_076077_0_0_4; -.
DR OMA; CCTPLQV; -.
DR BioCyc; NMEN122587:NMA_RS05610-MON; -.
DR UniPathway; UPA00501; -.
DR Proteomes; UP000000626; Chromosome.
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.
FT CHAIN 1..371
FT /note="N-acetyllactosaminide alpha-2,3-sialyltransferase"
FT /id="PRO_0000080573"
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; 42554 MW; F2D3F60DC588AC2B CRC64;
MGLKKACLTV LCLIVFCFGI FYTFDRVNQG ERNAVSLLKD KLFNEEGEPV NLIFCYTILQ
MKVAERIMAQ HPGERFYVVL MSENRNEKYD YYFNQIKDKA ERAYFFHLPY GLNKSFNFIP
TMAELKVKSM LLPKVKRIYL ASLEKVSIAA FLSTYPDAEI KTFDDGTGNL IQSSSYLGDE
FSVNGTIKRN FARMMIGDWS IAKTRNASDE HYTIFKGLKN IMDDGRRKMT YLPLFDASEL
KAGDETGGTV RILLGSPDKE MKEISEKAAK NFNIQYVAPH PRQTYGLSGV TTLNSPYVIE
DYILREIKKN PHTRYEIYTF FSGAALTMKD FPNVHVYALK PASLPEDYWL KPVYALFTQS
GIPILTFDDK D
