P72097 (LST_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Neisseria meningitidis serogroup B

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Keywords
Biological process	Lipopolysaccharide biosynthesis
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	transferase activity, transferring glycosyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 371

371

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase

PRO_0000080574

Natural variations

Natural variant

2

1

G → S in strain: M982B / NRCC 4725.

Natural variant

29

1

Q → H in strain: 406Y / NRCC 4030 and NRCC 4725.

Natural variant

40

1

E → D in strain: 406Y / NRCC 4030, M982B / NRCC 4725 and 126E / NRCC 4010.

Natural variant

94

1

N → K in strain: 406Y / NRCC 4030 and M982B / NRCC 4725.

Natural variant

102

1

R → W in strain: 126E / NRCC 4010.

Natural variant

129

1

S → A in strain: 126E / NRCC 4010.

Natural variant

168

1

G → I in strain: 126E / NRCC 4010.

Natural variant

242

1

T → A in strain: 406Y / NRCC 4030 and 126E / NRCC 4010.

Natural variant

273

1

K → N in strain: 406Y / NRCC 4030 and 126E / NRCC 4010.

Secondary structure

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371

Helix Strand Turn

Details...

Beta strand

50 – 55

6

Helix

58 – 70

13

Beta strand

74 – 83

10

Helix

87 – 99

13

Beta strand

100 – 107

8

Helix

122 – 131

10

Beta strand

136 – 141

6

Helix

144 – 147

4

Helix

149 – 153

5

Beta strand

158 – 163

6

Helix

167 – 170

4

Helix

173 – 177

5

Helix

179 – 181

3

Helix

187 – 204

18

Beta strand

210 – 214

5

Beta strand

224 – 231

8

Beta strand

249 – 254

6

Helix

259 – 261

3

Helix

262 – 272

11

Beta strand

276 – 278

3

Beta strand

290 – 292

3

Helix

299 – 309

11

Beta strand

314 – 321

8

Helix

324 – 328

5

Beta strand

334 – 341

8

Helix

346 – 348

3

Helix

351 – 359

9

Beta strand

364 – 367

4

Sequences

	Sequence		Length	Mass (Da)
	P72097 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 1C0E51DA3DAACD15	FASTA	371	42,611
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

D81143.

RefSeq

NP_273962.1. NC_003112.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YK4	X-ray	1.94	A	48-370	[»]
2YK5	X-ray	2.32	A	49-370	[»]
2YK6	X-ray	2.83	A	49-370	[»]
2YK7	X-ray	2.18	A	49-370	[»]

ModBase

Search...

Protein family/group databases

CAZy

GT52. Glycosyltransferase Family 52.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBNEIT00000010853; EBNEIP00000010473; EBNEIG00000010853.

GeneID

903043.

GenomeReviews

Gene locus NMB0922 in contig AE002098_GR.

KEGG

nme:NMB0922.

NMPDR

fig|122586.1.peg.896.

PATRIC

20357291. VBINeiMen85645_1159.

TIGR

NMB0922.

Phylogenomic databases

GeneTree

EBGT00050000021202.

HOGENOM

HBG576479.

OMA

ERIMAQH.

ProtClustDB

CLSK877808.

Enzyme and pathway databases

BioCyc

NMEN122586:NMB_0922-MONOMER.

Family and domain databases

InterPro

IPR012477. Glyco_transf_52.
[Graphical view]

KO

K00785.

Pfam

PF07922. Glyco_transf_52. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LST_NEIMB

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program