LSRK_SALTY
ID LSRK_SALTY Reviewed; 530 AA.
AC Q8ZKQ6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
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, ECO:0000269|PubMed:17274596, ECO:0000269|PubMed:23672516};
GN Name=lsrK {ECO:0000255|HAMAP-Rule:MF_02053}; OrderedLocusNames=STM4072;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION AS A KINASE.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=14622426; DOI=10.1046/j.1365-2958.2003.03781.x;
RA Taga M.E., Miller S.T., Bassler B.L.;
RT "Lsr-mediated transport and processing of AI-2 in Salmonella typhimurium.";
RL Mol. Microbiol. 50:1411-1427(2003).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17274596; DOI=10.1021/cb600444h;
RA Xavier K.B., Miller S.T., Lu W., Kim J.H., Rabinowitz J., Pelczer I.,
RA Semmelhack M.F., Bassler B.L.;
RT "Phosphorylation and processing of the quorum-sensing molecule autoinducer-
RT 2 in enteric bacteria.";
RL ACS Chem. Biol. 2:128-136(2007).
RN [4]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23672516; DOI=10.1021/ja4024989;
RA Zhu J., Hixon M.S., Globisch D., Kaufmann G.F., Janda K.D.;
RT "Mechanistic insights into the LsrK kinase required for autoinducer-2
RT quorum sensing activation.";
RL J. Am. Chem. Soc. 135:7827-7830(2013).
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:0000269|PubMed:14622426,
CC ECO:0000269|PubMed:17274596}.
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 ECO:0000269|PubMed:17274596, ECO:0000269|PubMed:23672516};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for (S)-4,5-dihydroxypentane-2,3-dione
CC {ECO:0000269|PubMed:23672516};
CC KM=150 uM for ATP {ECO:0000269|PubMed:23672516};
CC Note=kcat is 7.6 sec(-1). {ECO:0000269|PubMed:23672516};
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; AE006468; AAL22912.1; -; Genomic_DNA.
DR RefSeq; NP_462953.1; NC_003197.2.
DR RefSeq; WP_000113089.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKQ6; -.
DR SMR; Q8ZKQ6; -.
DR STRING; 99287.STM4072; -.
DR BindingDB; Q8ZKQ6; -.
DR ChEMBL; CHEMBL4523412; -.
DR PaxDb; Q8ZKQ6; -.
DR EnsemblBacteria; AAL22912; AAL22912; STM4072.
DR GeneID; 1255599; -.
DR KEGG; stm:STM4072; -.
DR PATRIC; fig|99287.12.peg.4292; -.
DR HOGENOM; CLU_009281_3_4_6; -.
DR PhylomeDB; Q8ZKQ6; -.
DR BioCyc; SENT99287:STM4072-MON; -.
DR BRENDA; 2.7.1.189; 5542.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW Cytoplasm; Kinase; Reference proteome; Transferase.
FT CHAIN 1..530
FT /note="Autoinducer-2 kinase"
FT /id="PRO_0000351599"
SQ SEQUENCE 530 AA; 57440 MW; B14DBE279B54C7EF CRC64;
MARLCTHTES GHYLMALDAG TGSVRAVIFD LQGKQIAVGQ AEWQHLAVPD VPGSMEFDLA
KNWQLACQCI RQALQKAAIP ATAIAAVSAC SMREGIVIYD SNGEPIWACA NVDARAAHEV
SELKELYDNT FEEEVYRCSG QTLALSAIPR LLWLAHHRPD IYHRASTVTM ISDWMAFMLS
GELAVDPSNA GTTGLLDLVT RNWKRSLLQM AGLRSDILSP VKETGTLLGH ISQKAAEQCD
LQAGTPVIVG GGDVQLGCLG LGVVRPAQTA VLGGTFWQQV VNLPAPVTDP NMNVRINPHV
IPGMVQTESI SFFTGLTMRW FRDAFCAEEK LIAERLGIDA YSLLEDMASR VPPGAYGVMP
IFSDVMRFKR WYHAAPSFIN LSIDPEKCNK ATLFRALEEN AAIVSACNLQ QIAAFSGVQA
DSLVFAGGGS KGKLWSQILA DVTGLTVHVP VVKEATALGC AIAAGVGVGV WPSLAETGEK
LVRWDREHKP NPENFAVYQQ AREKWQAVYQ DQRALVDGGL TTSLWKAPGL
