ID   LSRK_YERPG              Reviewed;         530 AA.
AC   A9R072;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=YpAngola_A0855;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX87889.1; -; Genomic_DNA.
DR   RefSeq; WP_012229133.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R072; -.
DR   SMR; A9R072; -.
DR   KEGG; ypg:YpAngola_A0855; -.
DR   PATRIC; fig|349746.12.peg.1806; -.
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_0000351603"
SQ   SEQUENCE   530 AA;  56981 MW;  535EBBE7E41F9700 CRC64;
     MSQLDTTTPS GDYLMALDAG TGSVRAVIFD LNGNQIAAGQ AEWLHLPVPD VPGSMEFDLT
     TNWQLTCQCI RQALHLAKLP ASAIRAVAAC SMREGIVLYD RSGTPIWACA NVDARASREV
     SELKELHNNG FELEIYQCSG QTLALSAMPR LLWLAHYRPD IYRQAGTLTM ISDWLANMLS
     GELAVDPSNA GTTGMLDLVT RNWQPNLLEM AGLRADILSP VKETGTLLGH VTAKAAQECG
     LLAGTPVVMG GGDVQLGCLG LGVVHAGQTA VLGGTFWQQV VNLPQPIIDP NMNTRINPHV
     IPGMVQAESI SFFTGLTMRW FRDAFCAEEK LLAQRLGIDT YSLLEDMAAR VPAGAYGVMP
     IFSDVMQFKS WYHAAPSFIN LSLDPEKCNK ATLFRALEEN AAIVSACNLA QIAEFSGVKA
     SSVVFAGGGA KGKLWSQILA DVTGVPVKVP VVKEATALGC AIAAGVGVGL YEALDKTGER
     LVRWEREYIP NTEHKALYQA AKTNWQAVYT DQLGLVDCGL TTSLWKAPGL