ID A0A090ILV8_9GAMM Unreviewed; 960 AA.
AC A0A090ILV8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AWOD_I_1729 {ECO:0000313|EMBL:CED71796.1};
OS Aliivibrio wodanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=80852 {ECO:0000313|EMBL:CED71796.1, ECO:0000313|Proteomes:UP000032427};
RN [1] {ECO:0000313|Proteomes:UP000032427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=06/09/139 {ECO:0000313|Proteomes:UP000032427};
RA Hjerde E.;
RL Submitted (SEP-2014) 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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; LN554846; CED71796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090ILV8; -.
DR STRING; 80852.AWOD_I_1729; -.
DR KEGG; awd:AWOD_I_1729; -.
DR PATRIC; fig|80852.17.peg.1783; -.
DR HOGENOM; CLU_000445_40_1_6; -.
DR Proteomes; UP000032427; Chromosome 1 complete sequence.
DR GO; GO:0016020; C: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; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd16172; TorS_sensor_domain; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.58.920; -; 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; IPR037952; Sensor_TorS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR014302; Sig_transdc_His_kinase_TorS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR038188; TorS_sensor_sf.
DR NCBIfam; TIGR02956; TMAO_torS; 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; PF00072; Response_reg; 1.
DR Pfam; PF21689; TorS_sensor_domain; 1.
DR PIRSF; PIRSF036437; HK_TorS; 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; 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 Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CED71796.1};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CED71796.1};
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..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 360..412
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 462..678
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 698..819
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 864..960
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 747
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 960 AA; 107724 MW; CD214B885354C71E CRC64;
MLFASTGIGR KLFLTFMVMI ALMAFGSVVG VLGFSYVEKT ERTVIDSAIP AVIEARYISD
LSTKIISTSQ LLSQVDSEAE RKKYGKELFS SIESLYVRLK GLGVYPFDKA LLTRLDRQVQ
DIVDNLATMG NNVGEKVVLH KKIQDKSKEL TQTALQLEEL ARSQVLNSNT ITIANVVKIY
DLVENENKDA IYKALDTLVE IDLDLAERLH ELRLLTFKVV NTIDDARNSN DISKVEKLRQ
DFTRDMTIIT RRVQAVEDPS RTRQMLMLAN RLTKSERLFS ELIQLVNINQ KLKSLSDENI
HQFQELNLII SQLLEQANDV TQQAVADVNF VLKLVQQLLI SITLLGLCLV IYIMWRYVYA
RVIMRLNQYE QAITDVANGQ LNIELDTSGD DELARMGRSI LIARDTAQEL KEYKDSLELQ
IAQRTQELKS SNELLNVEII NHDKARDLAE QANRAKSAFL ATMSHEIRTP LNGVLGTGEL
LRGSGLTAQQ KQYVDIINRS GENLLDLLND ILDYSKIEAG HLSIRAVNFN VHSMITDVQH
LFSSRAQQKG ITLAFDVPAD LPAWWIGDCT RIRQILNNFV GNAVKFTHTG SVTIQLHVIL
DTTLLFEVVD TGVGIAKHEI DSLFEAFTQA EEGQKVYGGT GLGLAISQRL IEAMDGEIGV
ESKEGLGSTF WFSLELEEGR CITVSNQEST VPEVASGHLL LVEDNPVNQM VAVGFLERLG
HKVTAVDTGF LAEEALKKEQ FDMLLLDINL PDTDGVTLQK RLRDIEQEKE GSNEYTPILA
VSAHVFDEDV ESYLAAGFDG FLAKPLVENQ LIKMLNRFLN DNHQQKGAEV PQEQLTLSVE
NNSAEEMEMI LNEKVLQSDL AVLGDERMLK IIALFRQSSK DNLSQLQKAI EERDTYQVNQ
LAHKLKGSAG SLGLMQLYKL CNSYEEMGKT GDISQCDNIE LEAVYRNSIL AVTHFFDRLN
//
