LSRK_ECOLI
ID LSRK_ECOLI Reviewed; 530 AA.
AC P77432; Q99894;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
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}; Synonyms=ydeV;
GN OrderedLocusNames=b1511, JW1504;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-495.
RX PubMed=8649811;
RA Das R., Reddy E.P., Chatterjee D., Andrews D.W.;
RT "Identification of a novel Bcl-2 related gene, BRAG-1, in human glioma.";
RL Oncogene 12:947-951(1996).
RN [5]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15601708; DOI=10.1128/jb.187.1.238-248.2005;
RA Xavier K.B., Bassler B.L.;
RT "Regulation of uptake and processing of the quorum-sensing autoinducer AI-2
RT in Escherichia coli.";
RL J. Bacteriol. 187:238-248(2005).
RN [6]
RP FUNCTION IN REGULATION.
RX PubMed=17557827; DOI=10.1128/jb.00014-07;
RA Li J., Attila C., Wang L., Wood T.K., Valdes J.J., Bentley W.E.;
RT "Quorum sensing in Escherichia coli is signaled by AI-2/LsrR: effects on
RT small RNA and biofilm architecture.";
RL J. Bacteriol. 189:6011-6020(2007).
RN [7]
RP FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=20025244; DOI=10.1021/cb9002738;
RA Roy V., Fernandes R., Tsao C.Y., Bentley W.E.;
RT "Cross species quorum quenching using a native AI-2 processing enzyme.";
RL ACS Chem. Biol. 5:223-232(2010).
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. Required for the regulation of the lsr operon and many
CC other genes. {ECO:0000269|PubMed:15601708, ECO:0000269|PubMed:17557827,
CC ECO:0000269|PubMed:20025244}.
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}.
CC -!- CAUTION: Was originally thought to originate from human and was called
CC BRAG1 (brain-related apoptosis gene 1) with a proposed role in
CC apoptosis (PubMed:8649811). The DNA sequence of the region sequenced is
CC more than 99% identical to that of this E.coli gene. Furthermore the
CC claim of an 'extensive similarity to the Bcl-2 family of genes' is not
CC correct. {ECO:0000305|PubMed:8649811}.
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DR EMBL; U00096; AAC74584.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15191.1; -; Genomic_DNA.
DR EMBL; S82185; AAC17184.1; -; mRNA.
DR PIR; B64905; B64905.
DR RefSeq; NP_416028.3; NC_000913.3.
DR RefSeq; WP_000113108.1; NZ_SSZK01000001.1.
DR PDB; 5YA0; X-ray; 3.00 A; A/B=1-530.
DR PDB; 5YA1; X-ray; 2.70 A; A/B=1-530.
DR PDB; 5YA2; X-ray; 2.70 A; A/B=1-530.
DR PDBsum; 5YA0; -.
DR PDBsum; 5YA1; -.
DR PDBsum; 5YA2; -.
DR AlphaFoldDB; P77432; -.
DR SMR; P77432; -.
DR BioGRID; 4260224; 14.
DR DIP; DIP-11687N; -.
DR IntAct; P77432; 13.
DR STRING; 511145.b1511; -.
DR jPOST; P77432; -.
DR PaxDb; P77432; -.
DR PRIDE; P77432; -.
DR EnsemblBacteria; AAC74584; AAC74584; b1511.
DR EnsemblBacteria; BAA15191; BAA15191; BAA15191.
DR GeneID; 946069; -.
DR KEGG; ecj:JW1504; -.
DR KEGG; eco:b1511; -.
DR PATRIC; fig|1411691.4.peg.756; -.
DR EchoBASE; EB3565; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_3_4_6; -.
DR InParanoid; P77432; -.
DR OMA; SDAMHFK; -.
DR PhylomeDB; P77432; -.
DR BioCyc; EcoCyc:G6798-MON; -.
DR BioCyc; MetaCyc:G6798-MON; -.
DR BRENDA; 2.7.1.189; 2026.
DR PRO; PR:P77432; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071518; F:autoinducer-2 kinase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
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 3D-structure; Cytoplasm; Kinase; Reference proteome; Transferase.
FT CHAIN 1..530
FT /note="Autoinducer-2 kinase"
FT /id="PRO_0000059566"
FT CONFLICT 490..495
FT /note="PDPEKH -> TRPGKA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:5YA1"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5YA1"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 269..285
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:5YA1"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 390..416
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 433..443
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:5YA1"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:5YA1"
FT HELIX 492..501
FT /evidence="ECO:0007829|PDB:5YA1"
SQ SEQUENCE 530 AA; 57545 MW; CBC3B1E7C8982063 CRC64;
MARLFTLSES KYYLMALDAG TGSIRAVIFD LEGNQIAVGQ AEWRHLAVPD VPGSMEFDLN
KNWQLACECM RQALHNAGIA PEYIAAVSAC SMREGIVLYN NEGAPIWACA NVDARAAREV
SELKELHNNT FENEVYRATG QTLALSAIPR LLWLAHHRSD IYRQASTITM ISDWLAYMLS
GELAVDPSNA GTTGLLDLTT RDWKPALLDM AGLRADILSP VKETGTLLGV VSSQAAELCG
LKAGTPVVVG GGDVQLGCLG LGVVRPAQTA VLGGTFWQQV VNLAAPVTDP EMNVRVNPHV
IPGMVQAESI SFFTGLTMRW FRDAFCAEEK LIAERLGIDT YTLLEEMASR VPPGSWGVMP
IFSDRMRFKT WYHAAPSFIN LSIDPDKCNK ATLFRALEEN AAIVSACNLQ QIADFSNIHP
SSLVFAGGGS KGKLWSQILA DVSGLPVNIP VVKEATALGC AIAAGVGAGI FSSMAETGER
LVRWERTHTP DPEKHELYQD SRDKWQAVYQ DQLGLVDHGL TTSLWKAPGL
