ID   LUXO_VIBCH              Reviewed;         455 AA.
AC   Q9KT84;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Regulatory protein LuxO;
GN   Name=luxO; OrderedLocusNames=VC_1021;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   INTERACTION WITH SIGMA-54.
RX   PubMed=9748465; DOI=10.1128/jb.180.19.5256-5259.1998;
RA   Klose K.E., Novik V., Mekalanos J.J.;
RT   "Identification of multiple sigma54-dependent transcriptional activators in
RT   Vibrio cholerae.";
RL   J. Bacteriol. 180:5256-5259(1998).
CC   -!- FUNCTION: Involved in the regulation of different processes depending
CC       on the cell density. Acts together with sigma-54 to repress, perhaps
CC       indirectly, some genes.
CC   -!- MISCELLANEOUS: In strain El Tor C6706, at low cell density, LuxO acts
CC       indirectly on virulence gene expression by repressing hapR This leads
CC       to the expression of virulence factors. In strain El Tor N16961, the
CC       hapR gene is inactive due to a natural frameshift mutation.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE003852; AAF94180.1; -; Genomic_DNA.
DR   PIR; C82250; C82250.
DR   RefSeq; NP_230666.1; NC_002505.1.
DR   RefSeq; WP_001888250.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KT84; -.
DR   SMR; Q9KT84; -.
DR   STRING; 243277.VC_1021; -.
DR   DNASU; 2614291; -.
DR   EnsemblBacteria; AAF94180; AAF94180; VC_1021.
DR   GeneID; 57739704; -.
DR   GeneID; 66939758; -.
DR   KEGG; vch:VC_1021; -.
DR   PATRIC; fig|243277.26.peg.975; -.
DR   eggNOG; COG2204; Bacteria.
DR   HOGENOM; CLU_000445_0_6_6; -.
DR   OMA; MPISMQV; -.
DR   BioCyc; VCHO:VC1021-MON; -.
DR   PHI-base; PHI:708; -.
DR   PRO; PR:Q9KT84; -.
DR   Proteomes; UP000000584; Chromosome 1.
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: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   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..455
FT                   /note="Regulatory protein LuxO"
FT                   /id="PRO_0000081115"
FT   DOMAIN          1..112
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          132..361
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         160..167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         223..232
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   455 AA;  50839 MW;  0D2D2D02B95EF872 CRC64;
     MVEDTASVAA LYRSYLTPLD IDINIVGTGR DAIESIGRRE PDLILLDLRL PDMTGMDVLY
     AVKEKSPDVP IVFMTAHGSI DTAVEAMRHG AQDFLIKPCE ADRLRVTVNN AIRKASKLKN
     DVDNKNQNYQ GFIGSSQTMQ AVYRTIDSAA SSKASIFITG ESGTGKEVCA EAIHAASKRG
     DKPFIAINCA AIPKDLIESE LFGHVKGAFT GAATERQGAA EAADGGTLFL DELCEMDLDL
     QTKLLRFIQT GTFQKVGSSK MKSVDVRFVC ATNRDPWKEV QEGRFREDLY YRLYVIPLHL
     PPLRARGDDV IEIAYSLLGF MSKEEGKDFV RLSAEVVERF RQYEWPGNVR QLQNVLRNVV
     VLNEGREITL DMLPPPLNQM SAPINRALPL AHENKVSVHE IFPLWMTEKQ AIEQAIEACD
     GNIPRAATYL DVSPSTIYRK LQTWNEKVKE KEKER