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Database: UniProt
Entry: A0A0F4RD77_9RHOB
LinkDB: A0A0F4RD77_9RHOB
Original site: A0A0F4RD77_9RHOB 
ID   A0A0F4RD77_9RHOB        Unreviewed;       792 AA.
AC   A0A0F4RD77;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=TW80_16485 {ECO:0000313|EMBL:KJZ17931.1};
OS   Loktanella sp. S4079.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Loktanella.
OX   NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ17931.1, ECO:0000313|Proteomes:UP000033741};
RN   [1] {ECO:0000313|EMBL:KJZ17931.1, ECO:0000313|Proteomes:UP000033741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4079 {ECO:0000313|EMBL:KJZ17931.1,
RC   ECO:0000313|Proteomes:UP000033741};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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   -!- 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:KJZ17931.1}.
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DR   EMBL; JXYE01000011; KJZ17931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4RD77; -.
DR   STRING; 579483.TW80_16485; -.
DR   PATRIC; fig|579483.3.peg.3393; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000033741; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000033741}.
FT   DOMAIN          33..86
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          164..236
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          239..291
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          285..357
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          425..650
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          673..789
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         723
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   792 AA;  86938 MW;  BA3E8825E5A30523 CRC64;
     MCLDLGLSDE LTTTGRYMTS REASLQSAFG TDLSTIFFEL LNQISEGLLI TDAPSGHEGH
     RIFFVNDALA KMMGYTPDEL IGASPLIFQG EQSDKATMEL VAAAKREGIP FVGKIVNYNK
     RGEPIHVLWK LNPVFSAEGE VIAWLSLKED LSTKLDLEVK AVDVNNRLGR LIETMGDGVL
     FWDTASGSVV WSDHLKSLLG LHGQQIPPTF TSYINCVIPE DRNRVNSTIR RSASTGKPFD
     VQHRIEVASG EQKTLWLRGQ PTDTSGTRSE RYVVVVRDIT DQMKAERRLL QAEEIANIGS
     WEIDLIQNTL YWSPQVFRIH GFEPNSFQPT VEWAIESYHP DHRNMVQTAV NDAIEHGVPF
     QFEAVIVRPD GTERNVLSEG FVDFTNEGKP RGLFGVFIDR TDIKAKEDVI TKTQRMDALG
     KFVGGVAHDF NNLLAVIMGN LEALEETTQT DNEKRRVKAA LKATEHGAEL THSLLAFVKK
     SPMRISNVNI VEQIEGMMPL MRRVLPSNIT ISLTRLNTDV WVLCDATILE ACILNLVVNA
     RDALPDGGKV VINVEKVEID EHANAQLGAS VAPGHFAAIS VNDNGTGMSS QQLHQAQEPF
     FTTKAGGVNK GTGLGLPRVL GFAEQSNGIF RLYSEPGKGT SAKIILPLSK NRGAPVKPLV
     SNGTNYDSIR GKRVLLVEDQ QAVLEILEDV ITSIGLDVEI AISGDDAYNR FGHDFSFSLV
     VTDVVMPGEL QGPDLVQKLR SDGASFSAIY ISGYMGDSSV SNDEMGEFDI KLTKPVTKKA
     LAQAILEALS TC
//
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