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Database: UniProt
Entry: B5RF99_SALG2
LinkDB: B5RF99_SALG2
Original site: B5RF99_SALG2 
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
//
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