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P72097 (LST_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase

Short name=Alpha 2,3-ST
Short name=Beta-galactoside alpha-2,3-sialyltransferase
EC=2.4.99.-
Alternative name(s):
Lipooligosaccharide sialyltransferase
Gene names
Name:lst
Ordered Locus Names:NMB0922
OrganismNeisseria meningitidis serogroup B
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers sialic acid from the substrate CMP-sialic acid donor to the terminal beta-D-galactosyl-1,4-acetyl-beta-D-glucosamine on the lacto-N-neotetraose branch of the lipooligosaccharide.

Catalytic activity

CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine.

Pathway

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Miscellaneous

Present in outer membrane vesicle formulations which are used as vaccines in human.

Sequence similarities

Belongs to the glycosyltransferase 52 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
PRO_0000080574

Natural variations

Natural variant21G → S in strain: M982B / NRCC 4725.
Natural variant291Q → H in strain: 406Y / NRCC 4030 and NRCC 4725.
Natural variant401E → D in strain: 406Y / NRCC 4030, M982B / NRCC 4725 and 126E / NRCC 4010.
Natural variant941N → K in strain: 406Y / NRCC 4030 and M982B / NRCC 4725.
Natural variant1021R → W in strain: 126E / NRCC 4010.
Natural variant1291S → A in strain: 126E / NRCC 4010.
Natural variant1681G → I in strain: 126E / NRCC 4010.
Natural variant2421T → A in strain: 406Y / NRCC 4030 and 126E / NRCC 4010.
Natural variant2731K → N in strain: 406Y / NRCC 4030 and 126E / NRCC 4010.

Secondary structure

....................................................... 371
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P72097 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 1C0E51DA3DAACD15

FASTA37142,611
        10         20         30         40         50         60 
MGLKKACLTV LCLIVFCFGI FYTFDRVNQG ERNAVSLLKE KLFNEEGEPV NLIFCYTILQ 

        70         80         90        100        110        120 
MKVAERIMAQ HPGERFYVVL MSENRNEKYD YYFNQIKDKA ERAYFFHLPY GLNKSFNFIP 

       130        140        150        160        170        180 
TMAELKVKSM LLPKVKRIYL ASLEKVSIAA FLSTYPDAEI KTFDDGTGNL IQSSSYLGDE 

       190        200        210        220        230        240 
FSVNGTIKRN FARMMIGDWS IAKTRNASDE HYTIFKGLKN IMDDGRRKMT YLPLFDASEL 

       250        260        270        280        290        300 
KTGDETGGTV RILLGSPDKE MKEISEKAAK NFKIQYVAPH PRQTYGLSGV TTLNSPYVIE 

       310        320        330        340        350        360 
DYILREIKKN PHTRYEIYTF FSGAALTMKD FPNVHVYALK PASLPEDYWL KPVYALFTQS 

       370 
GIPILTFDDK N 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae."
Gilbert M., Watson D.C., Cunningham A.-M., Jennings M.P., Young N.M., Wakarchuk W.W.
J. Biol. Chem. 271:28271-28276(1996) [PubMed: 8910446] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 406Y / NRCC 4030, M982B / NRCC 4725 and MC58 / NRCC 4728.
[2]Gilbert M., Michniewicz J.J., Watson D.C., Wakarchuk W.W.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 126E / NRCC 4010.
[3]"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58."
Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. expand/collapse author list , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.
Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC58 / Serogroup B.
[4]"Characterization of the protein content of a meningococcal outer membrane vesicle vaccine by polyacrylamide gel electrophoresis and mass spectrometry."
Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.
Hum. Vaccin. 1:80-84(2005) [PubMed: 17038831] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Proteomic analysis of a meningococcal outer membrane vesicle vaccine prepared from the group B strain NZ98/254."
Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.
Proteomics 6:3400-3413(2006) [PubMed: 16645985] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: NZ98/254 / Serogroup B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U60660 Genomic DNA. Translation: AAC44541.1.
U60661 Genomic DNA. Translation: AAC44543.1.
U60662 Genomic DNA. Translation: AAC44544.2.
U60663 Genomic DNA. Translation: AAC44545.1.
AE002098 Genomic DNA. Translation: AAF41330.1.
PIRD81143.
RefSeqNP_273962.1. NC_003112.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YK4X-ray1.94A48-370[»]
2YK5X-ray2.32A49-370[»]
2YK6X-ray2.83A49-370[»]
2YK7X-ray2.18A49-370[»]
ModBaseSearch...

Protein family/group databases

CAZyGT52. Glycosyltransferase Family 52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000010853; EBNEIP00000010473; EBNEIG00000010853.
GeneID903043.
GenomeReviewsGene locus NMB0922 in contig AE002098_GR.
KEGGnme:NMB0922.
NMPDRfig|122586.1.peg.896.
PATRIC20357291. VBINeiMen85645_1159.
TIGRNMB0922.

Phylogenomic databases

GeneTreeEBGT00050000021202.
HOGENOMHBG576479.
OMAERIMAQH.
ProtClustDBCLSK877808.

Enzyme and pathway databases

BioCycNMEN122586:NMB_0922-MONOMER.

Family and domain databases

InterProIPR012477. Glyco_transf_52.
[Graphical view]
KOK00785.
PfamPF07922. Glyco_transf_52. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLST_NEIMB
AccessionPrimary (citable) accession number: P72097
Secondary accession number(s): P72099, P72100, P72101
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families