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Database: UniProt
Entry: A0A1R1I8R8_9RHOO
LinkDB: A0A1R1I8R8_9RHOO
Original site: A0A1R1I8R8_9RHOO 
ID   A0A1R1I8R8_9RHOO        Unreviewed;       617 AA.
AC   A0A1R1I8R8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN   ORFNames=BJN45_08480 {ECO:0000313|EMBL:OMG55166.1};
OS   Azonexus hydrophilus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Azonexus.
OX   NCBI_TaxID=418702 {ECO:0000313|EMBL:OMG55166.1, ECO:0000313|Proteomes:UP000187526};
RN   [1] {ECO:0000313|EMBL:OMG55166.1, ECO:0000313|Proteomes:UP000187526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS02 {ECO:0000313|EMBL:OMG55166.1,
RC   ECO:0000313|Proteomes:UP000187526};
RA   Salah Z., Rout S.P., Humphreys P.N.;
RT   "Alkaliphiles isolated from bioreactors.";
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,
CC         ECO:0000256|PIRNR:PIRNR003167};
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}.
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:OMG55166.1}.
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DR   EMBL; MTHD01000002; OMG55166.1; -; Genomic_DNA.
DR   RefSeq; WP_076093959.1; NZ_MTHD01000002.1.
DR   AlphaFoldDB; A0A1R1I8R8; -.
DR   STRING; 418702.BJN45_08480; -.
DR   OrthoDB; 9811306at2; -.
DR   Proteomes; UP000187526; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd19408; NarX_NarQ_sensor; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 1.20.120.960; Histidine kinase NarX, sensor domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR029095; NarX-like_N.
DR   InterPro; IPR042295; NarX-like_N_sf.
DR   InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF13675; PilJ; 1.
DR   PIRSF; PIRSF003167; STHK_NarX/NarQ; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR003167};
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR003167};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR003167};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003167};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003167};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003167};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187526};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003167};
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,
KW   ECO:0000256|PIRNR:PIRNR003167}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          192..244
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          417..611
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          236..263
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   617 AA;  68204 MW;  D31268F96A43FDEE CRC64;
     MKRFVVSISQ ALHDSVLVRL GLAMGILALL SFASIVTSTV IAENISGQAS AINVSGSLRM
     MSFRSLSEVQ QPDKRAQALD TIEQFERRLH GLDRHVQSKT AGDSPSKQAI NVVTLRWTEH
     IRPIARAAAE GNGDALIQMA QDIPGFVQQI DYVVQLIEED LEHKVRWLRA TQFALLTLIL
     LVSLVTSWML RRQLVQPLAQ LLKAAKTVSR GSFSVRVRHV SGDELGQLGR AFNTMVAEIA
     SMYGNLEEKV DEKTRELTRT NESLELLYKV SQKLSASDLT LEQLQGILRE VESSLELGHS
     MICISDNGHL PAHPVVGDLT PDEVSKWCGQ QDCGQCFART SETLSQQAES SNVVVVPIGE
     AGGLQGTLPI MLRSRDPLPA DTARLIETVG HHVSNALINM RRTEEKHRLA VLEERSVIAR
     ELHDSIAQSL SYLRIQVTRL EKCIDQGCDA RTIAEELKDG LSSAYRELRE LITTFRLRID
     ERGFGVALEE TIAEFSTKLA FPVELHNTLS GIVLSGNEEM HVIRIIREAL SNIERHAGAT
     QAAVNISVDA EHSVCIRISD NGKGFNPAEI PENHFGTSIM RDRAHILEGE LSVDTAPGAG
     TTINLNFLPQ KYRQTEH
//
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