LSRK_YERPY
ID LSRK_YERPY Reviewed; 530 AA.
AC B1JLP8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=YPK_3648;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
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; CP000950; ACA69915.1; -; Genomic_DNA.
DR RefSeq; WP_012304621.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JLP8; -.
DR SMR; B1JLP8; -.
DR EnsemblBacteria; ACA69915; ACA69915; YPK_3648.
DR KEGG; ypy:YPK_3648; -.
DR PATRIC; fig|502800.11.peg.4402; -.
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_0000351609"
SQ SEQUENCE 530 AA; 57025 MW; 5744111469226506 CRC64;
MSQLDTTTPS GDYLMALDAG TGSVRAVIFD LNGNQIAAGQ AEWLHLPVPD VPGSMEFDLT
TNWQLMCQCI 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