LSRK_YERPP
ID LSRK_YERPP Reviewed; 530 AA.
AC A4TQL2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=YPDSF_3216;
OS Yersinia pestis (strain Pestoides F).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=386656;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pestoides F;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA Richardson P.;
RT "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL Submitted (FEB-2007) 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; CP000668; ABP41574.1; -; Genomic_DNA.
DR RefSeq; WP_002230543.1; NZ_CP009715.1.
DR AlphaFoldDB; A4TQL2; -.
DR SMR; A4TQL2; -.
DR GeneID; 66843026; -.
DR KEGG; ypp:YPDSF_3216; -.
DR PATRIC; fig|386656.14.peg.1127; -.
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_0000351602"
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