LUXQ_VIBPA
ID LUXQ_VIBPA Reviewed; 858 AA.
AC Q87GU5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Autoinducer 2 sensor kinase/phosphatase LuxQ;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
GN Name=luxQ; OrderedLocusNames=VPA1220;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- FUNCTION: At low cell density, in absence of autoinducer has a kinase
CC activity, and autophosphorylates on a histidine residue. The phosphoryl
CC group is then transferred to an aspartate residue in 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
CC autoinducer, the kinase activity is inactivated, and the response
CC regulator domain has a phosphatase activity (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Binds the complex formed by the autoinducer and LuxP.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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DR EMBL; BA000032; BAC62563.1; -; Genomic_DNA.
DR RefSeq; NP_800730.1; NC_004605.1.
DR RefSeq; WP_005477121.1; NC_004605.1.
DR AlphaFoldDB; Q87GU5; -.
DR SMR; Q87GU5; -.
DR STRING; 223926.28809588; -.
DR EnsemblBacteria; BAC62563; BAC62563; BAC62563.
DR GeneID; 1191916; -.
DR KEGG; vpa:VPA1220; -.
DR PATRIC; fig|223926.6.peg.4148; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_74_1_6; -.
DR OMA; IYACTAD; -.
DR Proteomes; UP000002493; Chromosome 2.
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; 3.30.450.220; -; 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; IPR015387; LuxQ-periplasm_dom.
DR InterPro; IPR043056; LuxQ-periplasm_N.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029151; Sensor-like_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; PF00512; HisKA; 1.
DR Pfam; PF09308; LuxQ-periplasm; 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; SSF103190; SSF103190; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..858
FT /note="Autoinducer 2 sensor kinase/phosphatase LuxQ"
FT /id="PRO_0000074784"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 488..710
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 735..850
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 491
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 784
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 858 AA; 96790 MW; E7EE42516CEDB5B7 CRC64;
MTITSKLKKR RSLSTLITKI IILVLAPIIL GIFVQSYYFS KQIIWQEVDR TKQQTSALIL
NIFESHFAAI QIHHDSNSKS DVILDFYSER NEEALNYFFL SIDQSDPSHT PEFRFLTDHQ
GIIWDDGNAH FYGINDSMLD GLTSKVTFSN NWYYVTSITS MGARHLLLRR VPVLEPKTGE
VMGYSYNAVV LDNNFALMEK LKNEGNVDNV VLVANDIPVA SSLAGDESYK IFDVLKRKET
QKKLDQLLII QTPIEVNAAI TNLKLLTVQD NQSVVTLQIQ HFLAMLASVI GMIMIALMTK
EWIENRVVEE LGSLMSYTRS AREEKGFERF GGSDIEEFDH IGSTLESTFE ELEAQKRSFR
DLFNFALSPI MVWSEAGVLI QINPAARKEL VIENDIETMH PVFKGFKDKL VPHLRMAAQG
ATLTGVNVPI GDKVFRWNLS PIRVDGDISG IIVQGQDITT LIEAEKQSNL ARREAEKSAQ
ARADFLAKMS HEIRTPINGI LGVAQLLKDS VEAEEQKNQI DVLRHSGEHL LAVLNDILDF
SKIEQGKFNI QKHPFSFADT MRTLENIYRP ICENKGVELV IENQLDGNVE IFTDQVRLNQ
ILFNLVSNAV KFTPSGCVRL HAELEQFYGA DNSVLVVEIS DTGIGIESDK LDEMFEPFVQ
EEATTTREYG GSGLGLTIVK NLVDMLDGDV QVRSQKGQGT TFVVTLPVKD RERVLAPLDS
SQRVKPAELF DESLKVLLVE DNHTNAFILK AFCTKYKMQV DWAKDGLEAM EFLKDHSYDL
ILMDNQLPHL GGIETTKEIR QNLKLGTPIY ACTADTAQET SDAFMEAGAN YVLLKPIKEN
ALHEAFVDFK QRFLIERT
