ID   LUXU_VIBHA              Reviewed;         114 AA.
AC   P0C5S4; Q9ZBB6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Phosphorelay protein LuxU;
GN   Name=luxU;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION AT HIS-58, AND
RP   MUTAGENESIS OF HIS-58 AND HIS-103.
RC   STRAIN=BB7;
RX   PubMed=9922254; DOI=10.1128/jb.181.3.899-906.1999;
RA   Freeman J.A., Bassler B.L.;
RT   "Sequence and function of LuxU: a two-component phosphorelay protein that
RT   regulates quorum sensing in Vibrio harveyi.";
RL   J. Bacteriol. 181:899-906(1999).
RN   [2]
RP   STRUCTURE BY NMR, AND SUBUNIT.
RX   PubMed=15740742; DOI=10.1016/j.jmb.2005.01.039;
RA   Ulrich D.L., Kojetin D., Bassler B.L., Cavanagh J., Loria J.P.;
RT   "Solution structure and dynamics of LuxU from Vibrio harveyi, a
RT   phosphotransferase protein involved in bacterial quorum sensing.";
RL   J. Mol. Biol. 347:297-307(2005).
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. {ECO:0000269|PubMed:9922254}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15740742}.
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DR   EMBL; L26221; AAD12737.2; -; Genomic_DNA.
DR   PDB; 1Y6D; NMR; -; A=1-114.
DR   PDBsum; 1Y6D; -.
DR   AlphaFoldDB; P0C5S4; -.
DR   BMRB; P0C5S4; -.
DR   SMR; P0C5S4; -.
DR   iPTMnet; P0C5S4; -.
DR   EvolutionaryTrace; P0C5S4; -.
DR   GO; GO:0004672; F:protein kinase activity; IEA:UniProt.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   DisProt; DP00292; -.
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   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Two-component regulatory system.
FT   CHAIN           1..114
FT                   /note="Phosphorelay protein LuxU"
FT                   /id="PRO_0000220141"
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,
FT                   ECO:0000269|PubMed:9922254"
FT   MUTAGEN         58
FT                   /note="H->A: Constitutive luminescence."
FT                   /evidence="ECO:0000269|PubMed:9922254"
FT   MUTAGEN         103
FT                   /note="H->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:9922254"
FT   TURN            4..9
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   HELIX           10..14
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   HELIX           16..40
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   TURN            41..44
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   HELIX           47..57
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   HELIX           59..67
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   HELIX           71..82
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   HELIX           84..88
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   TURN            94..99
FT                   /evidence="ECO:0007829|PDB:1Y6D"
FT   HELIX           100..112
FT                   /evidence="ECO:0007829|PDB:1Y6D"
SQ   SEQUENCE   114 AA;  12689 MW;  E61DFCE6CB2C8D98 CRC64;
     MNTDVLNQQK IEELSAEIGS DNVPVLLDIF LGEMDSYIGT LTELQGSEQL LYLKEISHAL
     KSSAASFGAD RLCERAIAID KKAKANQLQE QGMETSEMLA LLHITRDAYR SWTN