LST_NEIMB
ID LST_NEIMB Reviewed; 371 AA.
AC P72097; P72099; P72100; P72101;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase {ECO:0000305|PubMed:8910446};
DE EC=2.4.99.6 {ECO:0000269|PubMed:8910446};
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:21880735, ECO:0000303|PubMed:8910446};
DE Short=LOS sialyltransferase {ECO:0000303|PubMed:21880735, ECO:0000303|PubMed:8910446};
GN Name=lst {ECO:0000303|PubMed:8910446}; OrderedLocusNames=NMB0922;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=406Y / NRCC 4030, M982B / NRCC 4725, and MC58 / NRCC 4728;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=126E / NRCC 4010;
RA Gilbert M., Michniewicz J.J., Watson D.C., Wakarchuk W.W.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=MC58;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17038831; DOI=10.4161/hv.1.2.1651;
RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.;
RT "Characterization of the protein content of a meningococcal outer membrane
RT vesicle vaccine by polyacrylamide gel electrophoresis and mass
RT spectrometry.";
RL Hum. Vaccin. 1:80-84(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=NZ98/254 / Serogroup B;
RX PubMed=16645985; DOI=10.1002/pmic.200500821;
RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT prepared from the group B strain NZ98/254.";
RL Proteomics 6:3400-3413(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 49-370 IN COMPLEXES WITH CMP; CDP
RP AND THE SUBSTRATE ANALOG CMP-3-FLUORO-N-ACETYL-NEURAMINIC ACID, SUBUNIT,
RP MUTAGENESIS OF GLU-124; ASP-258; HIS-280 AND ARG-282, REACTION MECHANISM,
RP AND ACTIVE SITE.
RC STRAIN=126E / NRCC 4010;
RX PubMed=21880735; DOI=10.1074/jbc.m111.249920;
RA Lin L.Y., Rakic B., Chiu C.P., Lameignere E., Wakarchuk W.W., Withers S.G.,
RA Strynadka N.C.;
RT "Structure and mechanism of the lipooligosaccharide sialyltransferase from
RT Neisseria meningitidis.";
RL J. Biol. Chem. 286:37237-37248(2011).
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. In vitro, can use a number of
CC different synthetic acceptors with lactose or galactose as the
CC saccharide portion, but shows a strong preference for the N-
CC acetyllactosamine containing acceptor. {ECO:0000269|PubMed:8910446}.
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:0000269|PubMed:8910446};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:8910446};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipooligosaccharide
CC biosynthesis. {ECO:0000305|PubMed:8910446}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21880735}.
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 -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human. {ECO:0000269|PubMed:16645985,
CC ECO:0000269|PubMed:17038831}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 52 family.
CC {ECO:0000305}.
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DR EMBL; U60660; AAC44541.1; -; Genomic_DNA.
DR EMBL; U60661; AAC44543.1; -; Genomic_DNA.
DR EMBL; U60662; AAC44544.2; -; Genomic_DNA.
DR EMBL; U60663; AAC44545.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF41330.1; -; Genomic_DNA.
DR PIR; D81143; D81143.
DR RefSeq; NP_273962.1; NC_003112.2.
DR RefSeq; WP_002244089.1; NC_003112.2.
DR PDB; 2YK4; X-ray; 1.94 A; A=49-370.
DR PDB; 2YK5; X-ray; 2.32 A; A=49-370.
DR PDB; 2YK6; X-ray; 2.83 A; A=49-370.
DR PDB; 2YK7; X-ray; 2.18 A; A=49-370.
DR PDBsum; 2YK4; -.
DR PDBsum; 2YK5; -.
DR PDBsum; 2YK6; -.
DR PDBsum; 2YK7; -.
DR AlphaFoldDB; P72097; -.
DR SMR; P72097; -.
DR CAZy; GT52; Glycosyltransferase Family 52.
DR PaxDb; P72097; -.
DR EnsemblBacteria; AAF41330; AAF41330; NMB0922.
DR KEGG; nme:NMB0922; -.
DR PATRIC; fig|122586.8.peg.1159; -.
DR HOGENOM; CLU_076077_0_0_4; -.
DR OMA; CCTPLQV; -.
DR UniPathway; UPA00501; -.
DR EvolutionaryTrace; P72097; -.
DR Proteomes; UP000000425; 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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Glycosyltransferase;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase.
FT CHAIN 1..371
FT /note="N-acetyllactosaminide alpha-2,3-sialyltransferase"
FT /id="PRO_0000080574"
FT ACT_SITE 258
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21880735"
FT ACT_SITE 280
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:21880735"
FT BINDING 255
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000305|PubMed:21880735,
FT ECO:0007744|PDB:2YK7"
FT BINDING 278..282
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000305|PubMed:21880735,
FT ECO:0007744|PDB:2YK7"
FT BINDING 299..300
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000305|PubMed:21880735,
FT ECO:0007744|PDB:2YK7"
FT BINDING 322..323
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000305|PubMed:21880735,
FT ECO:0007744|PDB:2YK7"
FT VARIANT 2
FT /note="G -> S (in strain: M982B / NRCC 4725)"
FT VARIANT 29
FT /note="Q -> H (in strain: 406Y / NRCC 4030 and NRCC 4725)"
FT VARIANT 40
FT /note="E -> D (in strain: 406Y / NRCC 4030, M982B / NRCC
FT 4725 and 126E / NRCC 4010)"
FT VARIANT 94
FT /note="N -> K (in strain: 406Y / NRCC 4030 and M982B / NRCC
FT 4725)"
FT VARIANT 102
FT /note="R -> W (in strain: 126E / NRCC 4010)"
FT VARIANT 129
FT /note="S -> A (in strain: 126E / NRCC 4010)"
FT VARIANT 168
FT /note="G -> I (in strain: 126E / NRCC 4010)"
FT VARIANT 242
FT /note="T -> A (in strain: 406Y / NRCC 4030 and 126E / NRCC
FT 4010)"
FT VARIANT 273
FT /note="K -> N (in strain: 406Y / NRCC 4030 and 126E / NRCC
FT 4010)"
FT MUTAGEN 124
FT /note="E->A: Decreases the binding affinity for the donor
FT substrate (but not catalytic rate)."
FT /evidence="ECO:0000269|PubMed:21880735"
FT MUTAGEN 258
FT /note="D->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21880735"
FT MUTAGEN 280
FT /note="H->A: Decreases the rate of sialic acid transfer."
FT /evidence="ECO:0000269|PubMed:21880735"
FT MUTAGEN 282
FT /note="R->A: Decreases both the binding affinity for the
FT donor substrate and the rate of sialic acid transfer."
FT /evidence="ECO:0000269|PubMed:21880735"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2YK6"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:2YK7"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2YK4"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:2YK4"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:2YK4"
SQ SEQUENCE 371 AA; 42611 MW; 1C0E51DA3DAACD15 CRC64;
MGLKKACLTV LCLIVFCFGI FYTFDRVNQG ERNAVSLLKE KLFNEEGEPV NLIFCYTILQ
MKVAERIMAQ HPGERFYVVL MSENRNEKYD YYFNQIKDKA ERAYFFHLPY GLNKSFNFIP
TMAELKVKSM LLPKVKRIYL ASLEKVSIAA FLSTYPDAEI KTFDDGTGNL IQSSSYLGDE
FSVNGTIKRN FARMMIGDWS IAKTRNASDE HYTIFKGLKN IMDDGRRKMT YLPLFDASEL
KTGDETGGTV RILLGSPDKE MKEISEKAAK NFKIQYVAPH PRQTYGLSGV TTLNSPYVIE
DYILREIKKN PHTRYEIYTF FSGAALTMKD FPNVHVYALK PASLPEDYWL KPVYALFTQS
GIPILTFDDK N
