BGLK_LISMO
ID BGLK_LISMO Reviewed; 294 AA.
AC Q8Y3R9;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Beta-glucoside kinase;
DE EC=2.7.1.85;
GN Name=bglK; OrderedLocusNames=lmo2764;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=12110692; DOI=10.1074/jbc.m206397200;
RA Thompson J., Lichtenthaler F.W., Peters S., Pikis A.;
RT "Beta-glucoside kinase (BglK) from Klebsiella pneumoniae. Purification,
RT properties, and preparative synthesis of 6-phospho-beta-D-glucosides.";
RL J. Biol. Chem. 277:34310-34321(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of cellobiose to
CC produce cellobiose-6'-P. May have a dual role of kinase and
CC transcriptional regulator of the cellobiose-PTS operon.
CC {ECO:0000269|PubMed:12110692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-cellobiose = 6-phospho-beta-D-glucosyl-(1->4)-D-
CC glucose + ADP + H(+); Xref=Rhea:RHEA:21944, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17057, ChEBI:CHEBI:30616, ChEBI:CHEBI:58312,
CC ChEBI:CHEBI:456216; EC=2.7.1.85;
CC Evidence={ECO:0000269|PubMed:12110692};
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; AL591984; CAD00977.1; -; Genomic_DNA.
DR PIR; AC1420; AC1420.
DR RefSeq; NP_466286.1; NC_003210.1.
DR RefSeq; WP_009931557.1; NZ_CP023861.1.
DR PDB; 4HTL; X-ray; 1.64 A; A=1-294.
DR PDBsum; 4HTL; -.
DR AlphaFoldDB; Q8Y3R9; -.
DR SMR; Q8Y3R9; -.
DR STRING; 169963.lmo2764; -.
DR PaxDb; Q8Y3R9; -.
DR DNASU; 986173; -.
DR EnsemblBacteria; CAD00977; CAD00977; CAD00977.
DR GeneID; 986173; -.
DR KEGG; lmo:lmo2764; -.
DR PATRIC; fig|169963.11.peg.2833; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_0_2_9; -.
DR OMA; ANYDAHD; -.
DR PhylomeDB; Q8Y3R9; -.
DR BioCyc; LMON169963:LMO2764-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047700; F:beta-glucoside kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..294
FT /note="Beta-glucoside kinase"
FT /id="PRO_0000390476"
FT BINDING 5..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:4HTL"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:4HTL"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 121..138
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 209..233
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:4HTL"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:4HTL"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:4HTL"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4HTL"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:4HTL"
SQ SEQUENCE 294 AA; 32191 MW; 3191D8DD4345EA00 CRC64;
MKIAAFDIGG TALKMGVVLP HGEIILTKSA EISGSDGDQI LAEMKVFLAE NTDVTGIAVS
APGYVNPKTG LITMGGAIRR FDNFNLKEWL EAETGLPVAI ENDANCALLA EKWLGKGQDL
DDFLCLTIGT GIGGGIFSNG ELVRGGRFRA GEFGYMFSER PGAFRPGKYT LNETTTMLVL
RRQYAELTGR PLEEITGEEI FANYDAHDAV SERLITEFYT GICTGLYNLI YLFDPTHIFI
GGGITSRPTF IAELKHHMES FGLRDTIIET ATHKNQAGLL GAVYHFLQEE NRHE
