ID O68317_VIBCL Unreviewed; 1146 AA.
AC O68317;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=vieS {ECO:0000313|EMBL:AAC38448.1};
OS Vibrio cholerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=666 {ECO:0000313|EMBL:AAC38448.1};
RN [1] {ECO:0000313|EMBL:AAC38448.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C6709-1 {ECO:0000313|EMBL:AAC38448.1};
RX PubMed=9573178;
RA Lee S.H., Angelichio M.J., Mekalanos J.J., Camilli A.;
RT "Nucleotide sequence and spatiotemporal expression of the Vibrio cholerae
RT vieSAB genes during infection.";
RL J. Bacteriol. 180:2298-2305(1998).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AF031552; AAC38448.1; -; Genomic_DNA.
DR PIR; T09112; T09112.
DR AlphaFoldDB; O68317; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
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; cd00088; HPT; 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; 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 Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR019594; Glu/Gly-bd.
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; 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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00062; PBPb; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Kinase {ECO:0000313|EMBL:AAC38448.1};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:AAC38448.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 451..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 628..844
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 919..1037
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1042..1143
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 970
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1088
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1146 AA; 129484 MW; 737C683717988BC6 CRC64;
MPYWGGTGQE PIGIEHDFAS GIAKELGINI EYKGFDTIEA LLNAVSTGKA DMAIGFGQTL
AREGKFLFSK PLYENVRVIW LRDKAMEEKP FASLKWVCIQ GTSYCEILKD RGYPNIIMAR
NYSSSVEMIR QGIADATVTN YVSLNHYLSQ KRLALGKVIF DPDLGVQTNR ILINNNEPLL
LSAINKVIDA DKQGLTENKL NSADVYFLND QANLNILRNE NVNPVVRYTI QDDLFPMSYW
DEKEKKYKGY VHDLLERIST KSILKFEFVP AYGRDVEDML RHGKVDLIPS FNMTYVDDRY
FIHTGRYTDI QFGYIETTRP YTTPITGILD RTGKFNAYIA VQKNLSDVKV YRSMYDLEQA
LEKGDITHGL LNKVLINQML LDGHQDAFKL SPLTEGQDLR ADMTMLVRKD ARGLQNMLQK
VLATFSQQEI DEIKGAYDRV TVYFGYDKQK VLIYALIILC ALLSIGLILT LSLSRLRGKL
RSSEQVAKLS TEQLRWLTEL LDAIPSMIFI SDAKGEVVLT NAAYRKIYYT CCEKGCVQPQ
PECSFLALPD QHEAEFSIII QAPKSNCSIG EHYFHVTRRA ISHPINQRKY YLTLFNDITE
LKETEQALRQ SNEQALQAVE ARNHFLAVVS HELRTPIAAM LGLMEILASR LKSSESQLLL
TNAISSAERL KLHVNDILDF SKIEAQQLQL DIGLYNLADE LGPLLRGFEA SAQLKEIEFD
VIWSPNSLLL ANFDALRFNQ IVTNLLSNAI KFTDQGRVVF KIDVAPEMLT IAVEDTGCGM
TQTQIESLFV PFAQADSTIT RRFGGTGLGM SIVANLIELM NGKIEVKSEF EQGTQIQVNL
PLVTQTCDEF RGQVVAMSYR SPYMLWAKAL GMRVEENEEW VEQSGHNIYP DLLLNRLREV
SNLTQAQTEP AHSRLLQGHV LVADDDAINR LLIKKQLSEL GLSATLVSDG LQAFEKLSQH
PEQYDLLITD CHMPHLDGFA LTRKVKQEIS LFKGAVVGCT AEDSRLAAEQ ALQAGMDKVI
YKPYTLANLR KVLSRYLTTQ WVALPEQSWL DAYQEEEREE MAMVVAESLA QDIALLNQPD
CDVKALAHRI KGAAGSLQLQ RLADLAKTVE KQNDPQQLVA DKQQLINAMH EVVEQAQQWL
HQYQSE
//
