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Database: UniProt
Entry: E8XKD9_SALT4
LinkDB: E8XKD9_SALT4
Original site: E8XKD9_SALT4 
ID   E8XKD9_SALT4            Unreviewed;       530 AA.
AC   E8XKD9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Autoinducer-2 kinase {ECO:0000256|HAMAP-Rule:MF_02053};
DE            Short=AI-2 kinase {ECO:0000256|HAMAP-Rule:MF_02053};
DE            EC=2.7.1.189 {ECO:0000256|HAMAP-Rule:MF_02053};
GN   Name=lsrk {ECO:0000313|EMBL:ADX19847.1};
GN   Synonyms=lsrK {ECO:0000256|HAMAP-Rule:MF_02053};
GN   OrderedLocusNames=STM474_4254 {ECO:0000313|EMBL:ADX19847.1};
OS   Salmonella typhimurium (strain 4/74).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX19847.1, ECO:0000313|Proteomes:UP000008978};
RN   [1] {ECO:0000313|EMBL:ADX19847.1, ECO:0000313|Proteomes:UP000008978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978};
RX   PubMed=21478351; DOI=10.1128/JB.00394-11;
RA   Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA   Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT   "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT   Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT   animals.";
RL   J. Bacteriol. 193:3162-3163(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_02053};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02053}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_02053}.
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DR   EMBL; CP002487; ADX19847.1; -; Genomic_DNA.
DR   RefSeq; WP_000113090.1; NC_016857.1.
DR   AlphaFoldDB; E8XKD9; -.
DR   SMR; E8XKD9; -.
DR   KEGG; seb:STM474_4254; -.
DR   PATRIC; fig|909946.3.peg.4333; -.
DR   HOGENOM; CLU_009281_3_4_6; -.
DR   Proteomes; UP000008978; 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: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   Gene3D; 3.30.420.40; -; 2.
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; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   PANTHER; PTHR43095:SF1; AUTOINDUCER-2 KINASE; 1.
DR   PANTHER; PTHR43095; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02053};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02053, ECO:0000313|EMBL:ADX19847.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02053}.
FT   DOMAIN          13..260
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          299..466
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   530 AA;  57444 MW;  9060ECEED16E8AAE CRC64;
     MARLCTHTES GHYLMALDAG TGSVRAVIFD LQGKQIAVGQ AEWQHLAVPD VPGSMEFDLA
     KNWQLTCQCI RQALQKAAIP ATAIAAVSAC SMREGIVIYD SNGEPIWACA NVDARAAHEV
     SELKELHDNT 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
//
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