ID   LSRK_ECO57              Reviewed;         530 AA.
AC   Q8XAY5; Q7ADZ9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=Z2194, ECs2118;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG56255.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35541.1; -; Genomic_DNA.
DR   PIR; C85724; C85724.
DR   PIR; F90893; F90893.
DR   RefSeq; NP_310145.3; NC_002695.1.
DR   RefSeq; WP_000113137.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XAY5; -.
DR   SMR; Q8XAY5; -.
DR   STRING; 155864.EDL933_2127; -.
DR   EnsemblBacteria; AAG56255; AAG56255; Z2194.
DR   EnsemblBacteria; BAB35541; BAB35541; ECs_2118.
DR   GeneID; 917318; -.
DR   KEGG; ece:Z2194; -.
DR   KEGG; ecs:ECs_2118; -.
DR   PATRIC; fig|386585.9.peg.2224; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_4_6; -.
DR   OMA; SDAMHFK; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome; Transferase.
FT   CHAIN           1..530
FT                   /note="Autoinducer-2 kinase"
FT                   /id="PRO_0000351591"
SQ   SEQUENCE   530 AA;  57586 MW;  82EB0E0B0517B666 CRC64;
     MARLFTPSES KYYLMALDAG TGSIRAVIFD LEGNQIAVGQ AEWRHLAVPD VPGSMEFDLN
     KNWQLACECM RQALHNAGIA PEYIAAVSAC SMREGIVLYN NEGTPIWACA NVDARAAREV
     SELKELHNNT FENEVYRATG QTLALSAIPR LLWLAHHRSD IYRQASTITM ISDWLAYMLS
     GELAVDPSNA GTTGLLDLTI RDWKPALLDM AGLRADILSP VKETGTLLGV VSSQAAELCG
     LKVGTPVVVG GGDVQLGCLG LGVVRPAQTA VLGGTFWQQV VNLAAPVTDP EMNVRVNPHV
     IPGMVQAESI SFFTGLTMRW FRDAFCAEEK LIAERLGIDT YTLLEEMASR VPPGSWGVMP
     IFSDRMRFKT WYHAAPSFIN LSIDPDKCNK ATLFRALEEN AAIVSACNLQ QIADFSTIHP
     SSLVFAGGGS KGKLWSQILA DVSGLPVNIP VVKEATALGC AIAAGVGAGI FSSMAETGER
     LVRWERTHTP DPEKHELYQD SRDKWQAVYQ DQLGLVDHGL TTSLWKAPGL