Q8Y3R9 (BGLK_LISMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-glucoside kinase
EC=2.7.1.85

Gene names

Name:	bglK
Ordered Locus Names:	lmo2764

Organism

Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]

Taxonomic identifier

169963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria monocytogenes

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. May have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. Ref.2
Catalytic activity	ATP + cellobiose = ADP + 6-phospho-beta-D-glucosyl-(1->4)-D-glucose. Ref.2
Sequence similarities	Belongs to the ROK (NagC/XylR) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW beta-glucoside kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 294

294

Beta-glucoside kinase

PRO_0000390476

Regions

Nucleotide binding

5 – 11

7

ATP By similarity

Secondary structure

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294

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Beta strand

10 – 18

9

Beta strand

24 – 31

8

Helix

37 – 49

13

Beta strand

56 – 65

10

Turn

67 – 69

3

Beta strand

71 – 74

4

Helix

79 – 81

3

Helix

86 – 94

9

Beta strand

98 – 102

5

Helix

103 – 114

12

Turn

116 – 119

4

Beta strand

121 – 138

18

Helix

153 – 155

3

Beta strand

156 – 159

4

Helix

166 – 169

4

Helix

171 – 174

4

Helix

177 – 188

12

Helix

192 – 194

3

Helix

197 – 205

9

Helix

209 – 233

25

Beta strand

236 – 242

7

Helix

243 – 246

4

Helix

250 – 258

9

Turn

259 – 261

3

Beta strand

267 – 270

4

Turn

274 – 276

3

Helix

277 – 290

14

Sequences

	Sequence		Length	Mass (Da)
	Q8Y3R9 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 3191D8DD4345EA00	FASTA	294	32,191
	10 20 30 40 50 60 MKIAAFDIGG TALKMGVVLP HGEIILTKSA EISGSDGDQI LAEMKVFLAE NTDVTGIAVS 70 80 90 100 110 120 APGYVNPKTG LITMGGAIRR FDNFNLKEWL EAETGLPVAI ENDANCALLA EKWLGKGQDL 130 140 150 160 170 180 DDFLCLTIGT GIGGGIFSNG ELVRGGRFRA GEFGYMFSER PGAFRPGKYT LNETTTMLVL 190 200 210 220 230 240 RRQYAELTGR PLEEITGEEI FANYDAHDAV SERLITEFYT GICTGLYNLI YLFDPTHIFI 250 260 270 280 290 GGGITSRPTF IAELKHHMES FGLRDTIIET ATHKNQAGLL GAVYHFLQEE NRHE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e.
[2]	"Beta-glucoside kinase (BglK) from Klebsiella pneumoniae. Purification, properties, and preparative synthesis of 6-phospho-beta-D-glucosides." Thompson J., Lichtenthaler F.W., Peters S., Pikis A. J. Biol. Chem. 277:34310-34321(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION. Strain: ATCC BAA-679 / EGD-e.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL591984 Genomic DNA. Translation: CAD00977.1.

PIR

AC1420.

RefSeq

NP_466286.1. NC_003210.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4HTL	X-ray	1.64	A	1-294	[»]

ProteinModelPortal

Q8Y3R9.

ModBase

Search...

Protein-protein interaction databases

STRING

169963.lmo2764.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAD00977; CAD00977; CAD00977.

GeneID

986173.

KEGG

lmo:lmo2764.

PATRIC

20314835. VBILisMon69206_2833.

Organism-specific databases

GenoList

LMO2764.

Phylogenomic databases

eggNOG

COG1940.

HOGENOM

HOG000150087.

OMA

HYSIGID.

ProtClustDB

CLSK895075.

Enzyme and pathway databases

BioCyc

LMON169963:LMO2764-MONOMER.

Family and domain databases

InterPro

IPR000600. ROK.
[Graphical view]

Pfam

PF00480. ROK. 1 hit.
[Graphical view]

PROSITE

PS01125. ROK. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BGLK_LISMO

Accession

Primary (citable) accession number: Q8Y3R9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	March 1, 2002
Last modified:	May 29, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program