LUXO_VIBVY
ID LUXO_VIBVY Reviewed; 453 AA.
AC Q7MM78;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Regulatory protein LuxO;
GN Name=luxO; OrderedLocusNames=VV1195;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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 (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC93959.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000037; BAC93959.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q7MM78; -.
DR SMR; Q7MM78; -.
DR DIP; DIP-61931N; -.
DR STRING; 672.VV93_v1c11140; -.
DR EnsemblBacteria; BAC93959; BAC93959; BAC93959.
DR KEGG; vvy:VV1195; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_6_6; -.
DR OMA; MPISMQV; -.
DR Proteomes; UP000002675; Chromosome I.
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 3: Inferred from homology;
KW ATP-binding; DNA-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..453
FT /note="Regulatory protein LuxO"
FT /id="PRO_0000081120"
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; 50515 MW; 6090DAC72958C9D6 CRC64;
MVEDTASVAA LYRSYLMPLG IDINIVGTGR DAIDSLKHRI PDLILLDLRL PDMTGMDVLH
AVKASHPDVP IIFMTAHGSI DTAVEAMRHG SQDFLIKPCE ADRLRVTVNN AIRKASKLKN
DADSAGSQNY QGFIGSSQKM QQVYRTIDSA ASSKASIFIT GESGTGKEVC AEAIHAASRR
GDKPFIAINC AAIPKDLIES ELFGHVKGAF TGAATDRQGA AELADGGTLF LDELCEMDLD
LQTKLLRFIQ TGTFQKVGSS KMKSVDVRFV CATNRDPWKE VQEGRFREDL YYRLYVIPLH
LPPLRERGED VIEIAYSLLG YMSHEEGKNF VRFSQPVIDR FNEYEWPGNV RQLQNVLRNV
VVLNNGKEIT MEMLPPPLNQ PFERKESVQP DLSELISVRD ICPLWLTEKL AIEQAIKACD
GNIPRAAGYL DVSPSTIYRK LQAWNEKEEK QKA