ID   LUXU_VIBC1              Reviewed;         114 AA.
AC   A7MVC1; Q9ZBB6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Phosphorelay protein LuxU;
GN   Name=luxU; OrderedLocusNames=VIBHAR_02958;
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   POSSIBLE TRANSFER OF PHOSPHATE FROM LUXO TO LUXN VIA LUXU.
RX   PubMed=10632884; DOI=10.1046/j.1365-2958.2000.01684.x;
RA   Freeman J.A., Lilley B.N., Bassler B.L.;
RT   "A genetic analysis of the functions of LuxN: a two-component hybrid sensor
RT   kinase that regulates quorum sensing in Vibrio harveyi.";
RL   Mol. Microbiol. 35:139-149(2000).
CC   -!- FUNCTION: Phosphorelay protein which receives sensory signals from LuxN
CC       and LuxP and transmits them to LuxO, at low cell density. LuxN and LuxP
CC       transfer a phosphoryl group to LuxU on His-58 and this phosphoryl group
CC       is further transferred to LuxO. At high cell density, as LuxU could
CC       function to establish an equilibrium between the aspartyl-phosphate of
CC       LuxN and the aspartyl-phosphate of LuxO, LuxU transfers phosphate from
CC       LuxO to LuxN (and probably LuxP) and finally phosphate is drained from
CC       the system.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
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DR   EMBL; CP000789; ABU71911.1; -; Genomic_DNA.
DR   RefSeq; WP_012128493.1; NC_022269.1.
DR   AlphaFoldDB; A7MVC1; -.
DR   BMRB; A7MVC1; -.
DR   SMR; A7MVC1; -.
DR   EnsemblBacteria; ABU71911; ABU71911; VIBHAR_02958.
DR   KEGG; vha:VIBHAR_02958; -.
DR   PATRIC; fig|338187.25.peg.3227; -.
DR   OMA; TEMAYRE; -.
DR   OrthoDB; 1823523at2; -.
DR   Proteomes; UP000008152; Chromosome I.
DR   GO; GO:0004672; F:protein kinase activity; IEA:UniProt.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.160; -; 1.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   Pfam; PF01627; Hpt; 1.
DR   SUPFAM; SSF47226; SSF47226; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein; Two-component regulatory system.
FT   CHAIN           1..114
FT                   /note="Phosphorelay protein LuxU"
FT                   /id="PRO_0000310536"
FT   DOMAIN          19..114
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   MOD_RES         58
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   114 AA;  12689 MW;  E61DFCE6CB2C8D98 CRC64;
     MNTDVLNQQK IEELSAEIGS DNVPVLLDIF LGEMDSYIGT LTELQGSEQL LYLKEISHAL
     KSSAASFGAD RLCERAIAID KKAKANQLQE QGMETSEMLA LLHITRDAYR SWTN