ID   LUXO_VIBHA              Reviewed;         453 AA.
AC   P0C5S5; P54299;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Luminescence regulatory protein LuxO;
GN   Name=luxO;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB7;
RX   PubMed=8065259; DOI=10.1111/j.1365-2958.1994.tb01029.x;
RA   Bassler B.L., Wright M., Silverman M.R.;
RT   "Sequence and function of LuxO, a negative regulator of luminescence in
RT   Vibrio harveyi.";
RL   Mol. Microbiol. 12:403-412(1994).
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 (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; L26221; AAD12736.1; -; Genomic_DNA.
DR   PIR; S49540; S49540.
DR   AlphaFoldDB; P0C5S5; -.
DR   SMR; P0C5S5; -.
DR   STRING; 669.AL538_04125; -.
DR   PHI-base; PHI:4100; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008218; P:bioluminescence; IMP:CACAO.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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   3: Inferred from homology;
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_0000081117"
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:0000255|PROSITE-ProRule:PRU00169"
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