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Database: UniProt
Entry: A0A1I5RYR6_9RHOB
LinkDB: A0A1I5RYR6_9RHOB
Original site: A0A1I5RYR6_9RHOB 
ID   A0A1I5RYR6_9RHOB        Unreviewed;       892 AA.
AC   A0A1I5RYR6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04488047_109139 {ECO:0000313|EMBL:SFP63136.1};
OS   Tranquillimonas alkanivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=441119 {ECO:0000313|EMBL:SFP63136.1, ECO:0000313|Proteomes:UP000199356};
RN   [1] {ECO:0000313|EMBL:SFP63136.1, ECO:0000313|Proteomes:UP000199356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19547 {ECO:0000313|EMBL:SFP63136.1,
RC   ECO:0000313|Proteomes:UP000199356};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FOXA01000009; SFP63136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5RYR6; -.
DR   STRING; 441119.SAMN04488047_109139; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000199356; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
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:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 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; 3.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199356};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        55..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..254
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          251..328
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          329..383
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          456..508
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          521..744
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          764..880
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         814
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   892 AA;  96049 MW;  732ECD17BB505F8A CRC64;
     MKVTHGIVAP RVWLPVSAAL WLAAALLETL TPLGVTHGSL YLFPLMAVAA SGQRTPVIVV
     AALSAVATAA GFLVHEHGVS RSLELLDRAI TITLLGAFSV MALTLQEALA RARRGEAAAQ
     RSIEALARAE ATLQHAEGTG PIGSLHLDLA SGELRWSDGL FRIFGLESGG CLSMADVTAR
     LHPGDRAGFD NALSDALDRG ERLEHEHRIV RAGDGAVRRV ALIAEKVEGE GGAYLAGVVQ
     DVTDQRVRER RLRLLSSAVA MLDEIVLITE ADSLDSPEGP RIVYVNDAFE RITGYTREQA
     LGQTPRMLQG PCTQRAELDR LRAALEKAEP VSVELINYRA DGEEYWLEIS VSPVRDERGR
     LTHFVAVQRD VTRRKKNLEA LREVEERYRL VTQATSDVVW DWDMQTGGMW YSDSVLAMLG
     TRIDSLDAWL ARVHPDDRAH VEATNARMLE GADTVVEDEY RLRRADGTYI RVKDRAFVQR
     DAAGRPLRML GTMQDVTEAR EMEARLSRAE TLQAVGTLTG GVAHDINNLM TVVLGNADLL
     DEELEAQPGA RAKVDQIAGA AERAAALTGR LLAFAREQPL EPRSVDVPAL VEQLLPILRT
     SLPDSVSLRV QALPGLPPAH VDPGQLEVAL LNLVVNARDA MPRGGVIDIG ITFDRPDGRS
     DPLDGRPLPD ECLIVSVKDH GTGMTPEVLS KALDPFFTTK PPGAGTGLGL SMAYGFAKQS
     GGHIELSSTP RQGTTVRIFL PAASVPAIAR AARPDAPAAG GGEHVLLVED DRDVRAATER
     QLAALGYRVS SAEDAAEAMA ALEAHPDVAL LLTDLVLSGG MNGRELAERA REENPDLRVL
     YASGYAEAQV LAHDRPDPQV PLLRKPFRRA ALAAAVGGAL AGQSSSTETV RK
//
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