ID   LSRK_ECO24              Reviewed;         530 AA.
AC   A7ZLW9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Autoinducer-2 kinase {ECO:0000255|HAMAP-Rule:MF_02053};
DE            Short=AI-2 kinase {ECO:0000255|HAMAP-Rule:MF_02053};
DE            EC=2.7.1.189 {ECO:0000255|HAMAP-Rule:MF_02053};
GN   Name=lsrK {ECO:0000255|HAMAP-Rule:MF_02053};
GN   OrderedLocusNames=EcE24377A_1712;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_02053};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02053}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_02053}.
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DR   EMBL; CP000800; ABV16665.1; -; Genomic_DNA.
DR   RefSeq; WP_000113127.1; NC_009801.1.
DR   AlphaFoldDB; A7ZLW9; -.
DR   SMR; A7ZLW9; -.
DR   EnsemblBacteria; ABV16665; ABV16665; EcE24377A_1712.
DR   GeneID; 66674635; -.
DR   KEGG; ecw:EcE24377A_1712; -.
DR   HOGENOM; CLU_009281_3_4_6; -.
DR   OMA; SDAMHFK; -.
DR   Proteomes; UP000001122; 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:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
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   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; Carb_kinase_FGGY_C.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Kinase; Transferase.
FT   CHAIN           1..530
FT                   /note="Autoinducer-2 kinase"
FT                   /id="PRO_0000351590"
SQ   SEQUENCE   530 AA;  57529 MW;  CBC3B1E33BA1CC63 CRC64;
     MARLFTPSES KYYLMALDAG TGSIRAVIFD LEGNQIAVGQ AEWRHLAVPD VPGSMEFDLN
     KNWQLACECM RQALHNAGIA PEYIAAVSAC SMREGIVLYN NEGAPIWACA NVDARAAREV
     SELKELHNNT FENEVYRATG QTLALSAIPR LLWLAHHRSD IYRQASTITM ISDWLAYMLS
     GELAVDPSNA GTTGLLDLTT RDWKPALLDM AGLRADILSP VKETGTLLGV VSSQAAELCG
     LKAGTPVVVG GGDVQLGCLG LGVVRPAQTA VLGGTFWQQV VNLAAPVTDP EMNVRVNPHV
     IPGMVQAESI SFFTGLTMRW FRDAFCAEEK LIAERLGIDT YTLLEEMASR VPPGSWGVMP
     IFSDRMRFKT WYHAAPSFIN LSIDPDKCNK ATLFRALEEN AAIVSACNLQ QIADFSNIHP
     SSLVFAGGGS KGKLWSQILA DVSGLPVNIP VVKEATALGC AIAAGVGAGI FSSMAETGER
     LVRWERTHTP DPEKHELYQD SRDKWQAVYQ DQLGLVDHGL TTSLWKAPGL