LUXN_VIBC1
ID LUXN_VIBC1 Reviewed; 849 AA.
AC A7MRY4; P54301;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Autoinducer 1 sensor kinase/phosphatase LuxN;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
GN Name=luxN; OrderedLocusNames=VIBHAR_02766;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, PHOSPHORYLATION AT HIS-471 AND ASP-771, AND MUTAGENESIS OF
RP LEU-166; SER-468; ILE-469; HIS-471; ASN-475 AND ASP-771.
RX PubMed=10632884; DOI=10.1046/j.1365-2958.2000.01684.x;
RA Freeman J.A., Lilley B.N., Bassler B.L.;
RT "A genetic analysis of the functions of LuxN: a two-component hybrid sensor
RT kinase that regulates quorum sensing in Vibrio harveyi.";
RL Mol. Microbiol. 35:139-149(2000).
CC -!- FUNCTION: At low cell density, in the absence of AI-1 (autoinducer 1),
CC LuxN has a kinase activity and autophosphorylates on His-471. The
CC phosphoryl group is then transferred on Asp-771 of the response
CC regulator domain. The phosphoryl group is transferred to LuxU, and
CC ultimately to LuxO. At high cell density, in the presence of AI-1, the
CC kinase activity is inactivated, and the response regulator domain has a
CC phosphatase activity. LuxN phosphatase acts on itself. 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 finally phosphate is drained from the system.
CC {ECO:0000269|PubMed:10632884}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- ACTIVITY REGULATION: The phosphatase activity is constitutive and the
CC kinase activity is regulated by the presence or absence of AI-1. At low
CC cell density the kinase activity overrides the phosphatase activity.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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DR EMBL; CP000789; ABU71720.1; -; Genomic_DNA.
DR RefSeq; WP_012128348.1; NC_022269.1.
DR AlphaFoldDB; A7MRY4; -.
DR SMR; A7MRY4; -.
DR iPTMnet; A7MRY4; -.
DR EnsemblBacteria; ABU71720; ABU71720; VIBHAR_02766.
DR KEGG; vha:VIBHAR_02766; -.
DR PATRIC; fig|338187.25.peg.3410; -.
DR OMA; SNAYFHT; -.
DR OrthoDB; 1755994at2; -.
DR Proteomes; UP000008152; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; 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; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..849
FT /note="Autoinducer 1 sensor kinase/phosphatase LuxN"
FT /id="PRO_0000310535"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 468..683
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 722..835
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 471
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:10632884"
FT MOD_RES 771
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:10632884"
FT MUTAGEN 166
FT /note="L->R: Almost no light produced. Constitutive
FT luminescence; when associated with Q-471. Wild-type level
FT of light; when associated with A-771."
FT /evidence="ECO:0000269|PubMed:10632884"
FT MUTAGEN 468
FT /note="S->E: No effect."
FT /evidence="ECO:0000269|PubMed:10632884"
FT MUTAGEN 469
FT /note="I->G: Constitutive luminescence."
FT /evidence="ECO:0000269|PubMed:10632884"
FT MUTAGEN 471
FT /note="H->A,F,G,I,Q,R,S: Constitutive luminescence."
FT /evidence="ECO:0000269|PubMed:10632884"
FT MUTAGEN 471
FT /note="H->Q: Constitutive luminescence; when associated
FT with R-166."
FT /evidence="ECO:0000269|PubMed:10632884"
FT MUTAGEN 475
FT /note="N->R: Constitutive luminescence."
FT /evidence="ECO:0000269|PubMed:10632884"
FT MUTAGEN 771
FT /note="D->A: LuxN null phenotype. Wild-type level of light;
FT when associated with R-166."
FT /evidence="ECO:0000269|PubMed:10632884"
SQ SEQUENCE 849 AA; 96108 MW; 3E883198D05933B6 CRC64;
MFDFSLEAIV YAKAITLLAT VAVVMMWLFY YCYRLKQKNE VIFGTHHAAY IAYSVCIIAW
ISSNAYFHTD LLPELGASAG MFMAKFANLA SFFAFAFAYY FSCQLAAEQR KGKVHRWQQG
IFVSLTVYSL FINLRPGLTV EHVDIVGPSQ FIIEFGPHTS YFFIGLVSFV VLTLVNLVAM
RTNSSKLTLA KTNYMIAGIL VFMLSTAVIH LGMTYFMGDF SLTWLPPALS ISEMLFVGYA
LLTSRFYSVK YIAYLALSVL LVCAIFVLPL GAIFIPLTES NQWLIAIPIC ALIGITWQLL
YKKTSRYASF LIYGDKKTPV QQILSLEEDF KLSIDDAMRR LGKLLQIPND KLRLVTSNYN
ETFYEEYLSS NRSVLVFDEL SEELEYKVSA KRSMKALYDK MSSNNTALVM PLFGQGKSVT
HLLISPHKSN NQMFSNEEIS AVQTLLTRVQ STIEADRRIR QSRALANSIA HEMRNPLAQV
QLQFEALKQH IENHAPVEQI TLDIENGQAA IQRGRQLIDI ILREVSDSSP EHEPIAMTSI
HKAVDQAVSH YGFENEKIIE RIRLPQHTDF VAKLNETLFN FVIFNLIRNA IYYFDSYPDS
QIEISTKTGP YENTLIFRDT GPGIDETISH KIFDDFFSYQ KSGGSGLGLG YCQRVMRSFG
GRIECKSKLG TFTEFHLYFP VVPNAPKADT LRTPYFNDWK QNKRSNEHKV APNVQINNQS
PTVLIVDDKE VQRALVQMYL NQLGVNSLQA NNGENAVEVF KANHVDLILM DVQMPVMNGF
DASQRIKELS PQTPIVALSG ESGERELDMI NKLMDGRLEK PTTLNALRHV LGNWLNKNTA
SSACEAERE
