ID B5RF99_SALG2 Unreviewed; 530 AA.
AC B5RF99;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 82.
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=ydeV {ECO:0000313|EMBL:CAR39142.1};
GN Synonyms=lsrK {ECO:0000256|HAMAP-Rule:MF_02053};
GN OrderedLocusNames=SG3348 {ECO:0000313|EMBL:CAR39142.1};
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538 {ECO:0000313|EMBL:CAR39142.1, ECO:0000313|Proteomes:UP000008321};
RN [1] {ECO:0000313|EMBL:CAR39142.1, ECO:0000313|Proteomes:UP000008321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346 {ECO:0000313|Proteomes:UP000008321};
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Sanders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphrey T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933173; CAR39142.1; -; Genomic_DNA.
DR RefSeq; WP_000113085.1; NC_011274.1.
DR AlphaFoldDB; B5RF99; -.
DR SMR; B5RF99; -.
DR KEGG; seg:SG3348; -.
DR HOGENOM; CLU_009281_3_4_6; -.
DR OMA; SDAMHFK; -.
DR Proteomes; UP000008321; 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:CAR39142.1};
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; 57414 MW; F557A4814C8C4F99 CRC64;
MARLCTHTES GHYLMALDAG TGSVRAVIFD LQGKQIAVGQ AEWQHLAVPD VPGSMEFDLA
KNWQLACQCI 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
//