LUXO_VIBPA
ID LUXO_VIBPA Reviewed; 453 AA.
AC Q87MX7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Regulatory protein LuxO;
GN Name=luxO; OrderedLocusNames=VP2099;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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}.
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DR EMBL; BA000031; BAC60362.1; -; Genomic_DNA.
DR RefSeq; NP_798478.1; NC_004603.1.
DR AlphaFoldDB; Q87MX7; -.
DR SMR; Q87MX7; -.
DR STRING; 223926.28807092; -.
DR EnsemblBacteria; BAC60362; BAC60362; BAC60362.
DR KEGG; vpa:VP2099; -.
DR PATRIC; fig|223926.6.peg.2010; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_6_6; -.
DR OMA; MPISMQV; -.
DR Proteomes; UP000002493; 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 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_0000081118"
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; 50482 MW; A0A9CE20D91B4AFF 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
LPPLRERGED VIEIAYSLLG YMSHEEGKNF VRFSQEVIDR FNSYEWPGNV RQLQNVLRNI
VVLNNGKEIT LDMLPPPLNQ PLDRPSVSKL IEPKAMTVSE IMPLWMTEKM AIEQAIEACD
GNIPRAAGYL DVSPSTIYRK LQAWNGKEER QKV