ID E8LV52_9VIBR Unreviewed; 1052 AA.
AC E8LV52;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VIBR0546_14165 {ECO:0000313|EMBL:EGA65437.1};
OS Vibrio brasiliensis LMG 20546.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA65437.1, ECO:0000313|Proteomes:UP000004371};
RN [1] {ECO:0000313|EMBL:EGA65437.1, ECO:0000313|Proteomes:UP000004371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA65437.1,
RC ECO:0000313|Proteomes:UP000004371};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGA65437.1}.
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DR EMBL; AEVS01000071; EGA65437.1; -; Genomic_DNA.
DR AlphaFoldDB; E8LV52; -.
DR STRING; 945543.VIBR0546_14165; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000004371; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 163..233
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 309..530
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 549..671
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 696..818
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 864..962
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 603
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 751
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 903
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1052 AA; 117910 MW; E8E1123AEE4D3E50 CRC64;
MNSNSSFSFT VFNSDVARIA MRRKIASMLE VMGYSFQARD QLLVLGGEIM LRAFEQGETL
SVEVQVLTDS VAVTWAYQED EKSIQAFSIP LLNLTKSTKG LVWTLDSMVP ITEKVHTRLS
EIISEKSRDE LMHELRITNQ RLAQHQEGLE QEIELRTRDL QASEALSRTI IEGAPSSVAI
IDNKQRIILW NNTAEQTYGY RFEDIEGSNL CELLRIELPE ELKDILSGEL RFEDQSKVSG
GFFEVETYTS TGRMIPIDLG ITIFLFDDQC RAAMFLRDVT SRKAVEDELN QARSKAEEAV
EVKSMFLANM SHEIRTPMNA IIGMSHLALK TELTPKQHDY ISKIHNSASL LLGIINDILD
FSKIEAGKLS IETIEFHLDD VLHNVSMVTG QKAFEKGLEL IFQIDRDVPK VLYGDPLRLG
QIIINLVNNA VKFTEQGEIT VHVTRTPHSD QKVELKFSVQ DTGIGMSPEQ SDKLFSAFTQ
ADGSTTRRYG GTGLGLSICR RLVELMGGSI QVESILGQGS EFTFNVFTGF AEGDNAKSRV
VPQTLNDVKA MVVDDNEHAL LVMEDLLDVL PNAPSLVSSG ERAIAQLKQA AAEKQPYNLV
FMDWKMPGMS GIEATQKIRQ TLPDDARPKV VIVTAYDKED ISLDLEDLDV SGFLSKPVGQ
SYLFDLLMDL FGPTLDKEKN SHSTKRSKDS SLRGLRVLLV EDNEINQQIA VELMEEKGLK
VTVANNGQEA LDTLESTYQQ GSTSFEIIFM DLQMPVMDGY EAGTRIRADN RFDEIPLVAM
TAHAMIEERE RCLSIGMNDH VSKPIDPEVL FSTIKRCCSD YEATEQIEPA PAESSNDDGN
QQITTLEQVE SLDVKNGMLR VAGNEALYHR LLSQLIDKEY DFISRLDIAL EKQDYDYASL
ITHTLKGSAG NLGMVRLFDI AARLEHQLND SEQRTDIEPT KQELSDYIDP FFHQVCEGLG
RLYPSEVKNN LDDESVALIL QLDLLLNEFD ASAIEFLDEH YLRFNTLLKS EAFEVCCRHI
NDCDFLAASL ALRKAASIYP IDSEKMFGGT NG
//
