ID A0A427TZ81_9VIBR Unreviewed; 766 AA.
AC A0A427TZ81;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EJA03_17200 {ECO:0000313|EMBL:RSD29807.1};
OS Vibrio pectenicida.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=62763 {ECO:0000313|EMBL:RSD29807.1, ECO:0000313|Proteomes:UP000269041};
RN [1] {ECO:0000313|EMBL:RSD29807.1, ECO:0000313|Proteomes:UP000269041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 594 {ECO:0000313|EMBL:RSD29807.1,
RC ECO:0000313|Proteomes:UP000269041};
RA Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic taxonomy of the Vibrionaceae family.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RSD29807.1}.
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DR EMBL; RSFA01000107; RSD29807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427TZ81; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000269041; 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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; 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 PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RSD29807.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..225
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 247..468
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 491..609
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 663..760
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 540
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 702
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 766 AA; 85310 MW; F08BC31D2FC5D0A0 CRC64;
MSFRVKTILG IAFIEAVMLI ALTYSAMSFL SASNEKQLLQ RAHSTAEMFA LAAKDAMIST
DISTLDNLVK EFMTVEDISY IKVMHGDKEL SCAGDKALLD RSMNEDFTLG SVNDGIFDTR
REVKNAGVYY GTIDIGFEVS EINSMLTNAQ HSIIGIASIE VLLVSIFSFF LGTYLTKSLV
KLIQAANTVS EKGPGFQIND NSKDELGDVA RAFDDMSKKL EKSYKDLKTA RCEADEANDS
KSRFLASMSH EIRTPMNGVL GILDILEESK LSPEQKKLVN TATESGRFLL SVINDILDFT
RMESNTLRLE HKPFQFRRCV ESIVEVFLPT ARARSLDLSC TIDGSVPSDV YGDENRVKQV
LHNLIGNAIK FTKDGSVALQ IEAKSLNVGK SEITCKVIDT GIGINRNAMD YLFEEFTMAD
QTYSRSHEGS GLGLAICKRL CKLMDGHIKV ESTPSIGSTF SFSISLELAD KYIGVPLKPY
NNSELKVSDV SILVAEDNKA NQLVIQEMFN RLNLNVDIAE NGQRALEMIE LYHYDLIFMD
ISMPELDGIQ TCKQIRSNID PAINQIPVIA LTAHSLTGDK EMFLSAGMDD YLAKPVRLSQ
LIEKINLFLS DDSRECPSKR IDSSLESQVN PDNNDAEMDI QDTQVNLELV DETVLGQMIE
DTSVDVLPML IDHYLDESQQ RLQKIYQAMD DHDKDTLEFE THTLGSSALA LGNRVLSNLA
RKIEHLCIEN QEEQAYKLRD DLKELADNSL SALAYRKTQG FIEPAG
//
