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 02-SEP-2026, entry version 123. DE RecName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase {ECO:0000305|PubMed:8910446}; DE EC=2.4.3.6 {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 ATCC BAA-335 / MC58). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Neisseriaceae; 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=ATCC BAA-335 / 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=ATCC BAA-335 / 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=2.4.3.6; 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}. 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; 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; 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 AlphaFoldDB; P72097; -. DR SMR; P72097; -. DR STRING; 122586.NMB0922; -. DR CAZy; GT52; Glycosyltransferase Family 52. DR PaxDb; 122586-NMB0922; -. DR KEGG; nme:NMB0922; -. DR PATRIC; fig|122586.8.peg.1159; -. DR HOGENOM; CLU_076077_0_0_4; -. DR InParanoid; P72097; -. DR OrthoDB; 2339372at2; -. DR UniPathway; UPA00501; -. DR EvolutionaryTrace; P72097; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; EXP:UniProtKB. DR GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; EXP:UniProtKB. DR Gene3D; 3.30.370.20; -; 1. DR InterPro; IPR012477; Glyco_transf_52. DR Pfam; PF07922; Glyco_transf_52; 1. DR PDBsum; 2YK4; -. DR PDBsum; 2YK5; -. DR PDBsum; 2YK6; -. DR PDBsum; 2YK7; -. 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 119..121 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 //