LUXO_VIBC1
ID LUXO_VIBC1 Reviewed; 453 AA.
AC A7MVC2; P54299;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Luminescence regulatory protein LuxO;
GN Name=luxO; OrderedLocusNames=VIBHAR_02959;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND MUTAGENESIS OF ASP-4; ASP-47; PHE-94 AND LYS-97.
RX PubMed=10027982; DOI=10.1046/j.1365-2958.1999.01208.x;
RA Freeman J.A., Bassler B.L.;
RT "A genetic analysis of the function of LuxO, a two-component response
RT regulator involved in quorum sensing in Vibrio harveyi.";
RL Mol. Microbiol. 31:665-677(1999).
RN [3]
RP INTERACTION WITH SIGMA-54.
RX PubMed=10844680; DOI=10.1046/j.1365-2958.2000.01913.x;
RA Lilley B.N., Bassler B.L.;
RT "Regulation of quorum sensing in Vibrio harveyi by LuxO and sigma-54.";
RL Mol. Microbiol. 36:940-954(2000).
CC -!- FUNCTION: Acts negatively to control the expression of luminescence. At
CC low cell density, LuxO is phosphorylated, and together with sigma-54,
CC causes repression of the luxCDABEGH operon. This repression could be
CC indirect, LuxO could activate a negative regulator of luminescence. At
CC high cell density, LuxO is dephosphorylated and inactive, therefore the
CC luxCDABEGH operon is not repressed and light is emitted. LuxO and
CC sigma-54 have also a role in activating the production of siderophore
CC and in regulating the rugose colony morphology phenotype.
CC {ECO:0000269|PubMed:10027982}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABU71912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000789; ABU71912.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A7MVC2; -.
DR SMR; A7MVC2; -.
DR EnsemblBacteria; ABU71912; ABU71912; VIBHAR_02959.
DR KEGG; vha:VIBHAR_02959; -.
DR PATRIC; fig|338187.36.peg.2888; -.
DR Proteomes; UP000008152; Chromosome I.
DR CollecTF; EXPREG_00000270; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; EXP:CollecTF.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Nucleotide-binding; Phosphoprotein; Repressor;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..453
FT /note="Luminescence regulatory protein LuxO"
FT /id="PRO_0000310534"
FT DOMAIN 1..112
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 133..362
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 224..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 47
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT MUTAGEN 4
FT /note="D->K: Constitutive luminescence."
FT /evidence="ECO:0000269|PubMed:10027982"
FT MUTAGEN 47
FT /note="D->A,N: Constitutive luminescence."
FT /evidence="ECO:0000269|PubMed:10027982"
FT MUTAGEN 47
FT /note="D->E: Almost no light produced."
FT /evidence="ECO:0000269|PubMed:10027982"
FT MUTAGEN 94
FT /note="F->W: Almost no light produced."
FT /evidence="ECO:0000269|PubMed:10027982"
FT MUTAGEN 97
FT /note="K->A: Constitutive luminescence."
FT /evidence="ECO:0000269|PubMed:10027982"
SQ SEQUENCE 453 AA; 50459 MW; 0005EEA6F09339ED CRC64;
MVEDTASVAA LYRSYLTPLG IDINIVGTGR DAIESLNHRI PDLILLDLRL PDMTGMDVLH
AVKKSHPDVP IIFMTAHGSI DTAVEAMRHG SQDFLIKPCE ADRLRVTVNN AIRKATKLKN
EADNPGNQNY QGFIGSSQTM QQVYRTIDSA ASSKASIFIT GESGTGKEVC AEAIHAASKR
GDKPFIAINC AAIPKDLIES ELFGHVKGAF TGAANDRQGA AELADGGTLF LDELCEMDLD
LQTKLLRFIQ TGTFQKVGSS KMKSVDVRFV CATNRDPWKE VQEGRFREDL YYRLYVIPLH
LPPLRERGKD VIEIAYSLLG YMSHEEGKSF VRFAQDVIER FNSYEWPGNV RQLQNVLRNI
VVLNNGKEIT LDMLPPPLNQ PVVRQSVAKF IEPDIMTVSD IMPLWMTEKM AIEQAIQACE
GNIPRAAGYL DVSPSTIYRK LQAWNSKDEK QNV
