ID   LSRK_ECOLC              Reviewed;         530 AA.
AC   B1IRU9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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}; OrderedLocusNames=EcolC_2147;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA77787.1; -; Genomic_DNA.
DR   RefSeq; WP_000113150.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IRU9; -.
DR   SMR; B1IRU9; -.
DR   KEGG; ecl:EcolC_2147; -.
DR   HOGENOM; CLU_009281_3_4_6; -.
DR   OMA; SDAMHFK; -.
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_0000351587"
SQ   SEQUENCE   530 AA;  57572 MW;  7FBB7DFE6957B405 CRC64;
     MARLFTPSES KYYLMALDAG TGSIRAVIFD LEGNQIAVGQ AEWRHLAVPD VPGSMEFDLN
     KNWQLACECM RQALHNAGIA PEYIAAVSAC SMREGIVLYN NEGTPIWACA NVDARAAREV
     SELKELHNNT FENEVYRATG QTLALSAIPR LLWLAHHRSD IYRQASTITM ISDWLAYMLS
     GELAVDPSNA GTTGLLDLTT RNWKPALLDM AGLRADILSP VKETGTLLGV VSSQAAELCG
     LKAGTPVVVG GGDVQLGCLG LGVVRPAQTA VLGGTFWQQV VNLAAPVTDP EMNVRVNPHV
     IPGMVQAESI SFFTGLTMRW FRDAFCAEEK LIAERLGIDT YTLLEEMASR VPPGSWGVMP
     IFSDRMRFKT WYHAAPSFIN LSIDPDKCNK ATLFRALEEN AAIVSACNLQ QIADFSNIHP
     TSLVFAGGGS KGKLWSQILA DVSGLPVNIP VVKEATALGC AIAAGVGAGI FSSMAETGER
     LVRWERTHTP DPEKHELYQD SRDKWQAVYQ DQLGLVDHGL TTSLWKAPGL