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 27-MAR-2024, entry version 90. 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; Bacillota; 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}. 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; 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.gene:17595481; -. DR PaxDb; 169963-lmo2764; -. 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 OrthoDB; 9795247at2; -. DR PhylomeDB; Q8Y3R9; -. DR BioCyc; LMON169963:LMO2764-MONOMER; -. 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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR000600; ROK. DR PANTHER; PTHR18964:SF165; BETA-GLUCOSIDE KINASE; 1. DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1. DR Pfam; PF00480; ROK; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 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 //