ID   LSRK_YERPS              Reviewed;         530 AA.
AC   Q66EY7;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=YPTB0554;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19794.1; -; Genomic_DNA.
DR   RefSeq; WP_002230543.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66EY7; -.
DR   SMR; Q66EY7; -.
DR   EnsemblBacteria; CAH19794; CAH19794; YPTB0554.
DR   GeneID; 66843026; -.
DR   KEGG; ypo:BZ17_2005; -.
DR   KEGG; yps:YPTB0554; -.
DR   PATRIC; fig|273123.14.peg.2130; -.
DR   OMA; SDAMHFK; -.
DR   Proteomes; UP000001011; 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_0000351606"
SQ   SEQUENCE   530 AA;  56995 MW;  88BB91FEC3F7DAF9 CRC64;
     MSQLDTTTPS GDYLMALDAG TGSVRAVIFD LNGNQIAAGQ AEWLHLPVPD VPGSMEFDLT
     TNWQLTCQCI RQALHLAKLP ASAIRAVAAC SMREGIVLYD RSGTPIWACA NVDARASREV
     SELKELHNNG FELEVYQCSG QTLALSAMPR LLWLAHYRPD IYRQAGTLTM ISDWLANMLS
     GELAVDPSNA GTTGMLDLVT RNWQPNLLEM AGLRADILSP VKETGTLLGH VTAKAAQECG
     LLAGTPVVMG GGDVQLGCLG LGVVHAGQTA VLGGTFWQQV VNLPQPIIDP NMNTRINPHV
     IPGMVQAESI SFFTGLTMRW FRDAFCAEEK LLAQRLGIDT YSLLEDMAAR VPAGAYGVMP
     IFSDVMRFKS WYHAAPSFIN LSLDPEKCNK ATLFRALEEN AAIVSACNLA QIAEFSGVKA
     SSVVFAGGGA KGKLWSQILA DVTGVPVKVP VVKEATALGC AIAAGVGVGL YEALDKTGER
     LVRWEREYIP NTEHKALYQA AKTNWQAVYT DQLGLVDCGL TTSLWKAPGL