ID B7LRE3_ESCF3 Unreviewed; 530 AA.
AC B7LRE3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Autoinducer-2 kinase {ECO:0000256|HAMAP-Rule:MF_02053};
DE Short=AI-2 kinase {ECO:0000256|HAMAP-Rule:MF_02053};
DE EC=2.7.1.189 {ECO:0000256|HAMAP-Rule:MF_02053};
GN Name=lsrK {ECO:0000256|HAMAP-Rule:MF_02053,
GN ECO:0000313|EMBL:CAQ89085.1};
GN OrderedLocusNames=EFER_1566 {ECO:0000313|EMBL:CAQ89085.1};
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ89085.1, ECO:0000313|Proteomes:UP000000745};
RN [1] {ECO:0000313|Proteomes:UP000000745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC {ECO:0000313|Proteomes:UP000000745};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes the phosphorylation of autoinducer-2 (AI-2) to
CC phospho-AI-2, which subsequently inactivates the transcriptional
CC regulator LsrR and leads to the transcription of the lsr operon.
CC Phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione
CC (DPD), which is the precursor to all AI-2 signaling molecules, at the
CC C5 position. {ECO:0000256|HAMAP-Rule:MF_02053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4,5-dihydroxypentane-2,3-dione + ATP = (2S)-2-hydroxy-3,4-
CC dioxopentyl phosphate + ADP + H(+); Xref=Rhea:RHEA:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29484, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:71677, ChEBI:CHEBI:456216; EC=2.7.1.189;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02053};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02053}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_02053}.
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DR EMBL; CU928158; CAQ89085.1; -; Genomic_DNA.
DR RefSeq; WP_000113169.1; NC_011740.1.
DR AlphaFoldDB; B7LRE3; -.
DR GeneID; 75057391; -.
DR KEGG; efe:EFER_1566; -.
DR HOGENOM; CLU_009281_3_4_6; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000000745; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071518; F:autoinducer-2 kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009372; P:quorum sensing; IEA:InterPro.
DR CDD; cd07775; FGGY_AI-2K; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_02053; LsrK; 1.
DR InterPro; IPR033676; AI-2_kinase.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR PANTHER; PTHR43095:SF1; AUTOINDUCER-2 KINASE; 1.
DR PANTHER; PTHR43095; SUGAR KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02053};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02053, ECO:0000313|EMBL:CAQ89085.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02053}.
FT DOMAIN 13..260
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 298..467
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 530 AA; 57530 MW; 72A45FA21BDD9914 CRC64;
MARLFTPSES RHYLMALDAG TGSIRAVIFD LEGNQIAVGQ AEWRHLAVPD VPGSMEFDLN
KNWQLACECM RQALHNSGIA PEYIAAVSAC SMREGIVLYN NEGTPIWACA NVDARAAREV
SELKELHNNT FENEVYRATG QTLALSAIPR LLWLAHHRSD IYRQASTITM ISDWLAYMLS
GELAVDPSNA GTTGLLDLST RNWKPALLDM AGLRADILSP VKETGTLLGV VSSQAAELCG
LKAGTPVVVG GGDVQLGCLG LGVVRPTQTA VLGGTFWQQV VNLAAPVTDP EMNVRVNPHV
IPGMVQAESI SFFTGLTMRW FRDAFCAEEK LIAERLGIDT YTLLEEMASR VPPGSWGVMP
IFSDKMRFKT WYHAAPSFIN LSIDPDKCNK ATLFRALEEN AAIVSACNLQ QIADFSNIHP
TSLVFAGGGS KGKLWSQILA DVSGLPVNIP VVKEATALGC AIAAGVGAGI FSSLAEAGER
LVRWERTHTP DPEKHELYQD SRDKWQAVYQ DQLGLVDHGL TTSLWKAPGL
//
