ID B6VKP9_PHOAA Unreviewed; 530 AA.
AC B6VKP9; C7BTA3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
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:0000256|HAMAP-Rule:MF_02053};
GN OrderedLocusNames=PAU_01471 {ECO:0000313|EMBL:CAQ83563.1};
GN ORFNames=PA-RVA3-4013 {ECO:0000313|EMBL:CAR66729.1};
OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS (Xenorhabdus luminescens (strain 2)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=553480 {ECO:0000313|EMBL:CAR66729.1};
RN [1] {ECO:0000313|EMBL:CAR66729.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43949 {ECO:0000313|EMBL:CAR66729.1};
RX PubMed=18838673; DOI=10.1073/pnas.0711114105;
RA Waterfield N.R., Sanchez-Contreras M., Eleftherianos I., Dowling A.,
RA Wilkinson P., Parkhill J., Thomson N., Reynolds S.E., Bode H.B., Dorus S.,
RA Ffrench-Constant R.H.;
RT "Rapid virulence annotation (RVA): identification of virulence factors
RT using a bacterial genome library and multiple invertebrate hosts.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15967-15972(2008).
RN [2] {ECO:0000313|EMBL:CAQ83563.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC43949 {ECO:0000313|EMBL:CAQ83563.1};
RA Crossman L.C.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAR66729.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43949 {ECO:0000313|EMBL:CAR66729.1};
RA Thomson N.R.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CAQ83563.1, ECO:0000313|Proteomes:UP000002747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747}, and
RC ATCC43949 {ECO:0000313|EMBL:CAQ83563.1};
RX PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT "Comparative genomics of the emerging human pathogen Photorhabdus
RT asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL BMC Genomics 10:302-302(2009).
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; FM162591; CAQ83563.1; -; Genomic_DNA.
DR EMBL; FM211045; CAR66729.1; -; Genomic_DNA.
DR AlphaFoldDB; B6VKP9; -.
DR STRING; 291112.PAU_01471; -.
DR KEGG; pay:PAU_01471; -.
DR eggNOG; COG1070; Bacteria.
DR Proteomes; UP000002747; 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};
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 284..466
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 530 AA; 57419 MW; 2E67AFB7F93DE07F CRC64;
MNQRRSANPS GKYLMALDAG TGSVRAVIFD LEGNQIATGQ AEWAHQPVPD VPGSMEFDLV
MNWQLACQCI RQALKKAELP ACAIQGVASC SMREGIVLYN RNGEPIWACA NVDARSSHEV
GELKALYNNT FEYDVYQRSG QTLALGAMPR LLWLAHHRPD IYRQAAALTM ISDWLANMLS
GELAVDPSNA GTTGMLDLVS RDWCTNLLEM AGLRSDILSP VKETGTLLGY VTEKAASQCG
LDVGTPVIMG GGDVQLGCLG LGVVKPAQTA VIGGTFWQQV VNLPAPITDP NMNTRINPHV
IPGMVQAESI SFFTGLTMRW FRDAFCAEEK LLAERLGVDA YSLLEDMAAR VPAGAYGIMP
IFSDVMRFKA WYHAAPSFIN LSIDPEKCNK STLFRALEEN AAIVSACNLD LISAFSAVKL
DSLVFAGGGS KGKLWSQILS DVTGLPVRVP IVKESTALGC AIAAGVGVGL YDAMGATGEK
LVRWQHEYQP NPEHYEVYQK AKENWQAIYA DQLTLVDHGL TTSLWKAPGL
//
