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Database: UniProt
Entry: A0A246K0F9_9SPHN
LinkDB: A0A246K0F9_9SPHN
Original site: A0A246K0F9_9SPHN 
ID   A0A246K0F9_9SPHN        Unreviewed;       657 AA.
AC   A0A246K0F9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CDQ92_02050 {ECO:0000313|EMBL:OWQ98983.1};
OS   Sphingopyxis bauzanensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=651663 {ECO:0000313|EMBL:OWQ98983.1, ECO:0000313|Proteomes:UP000197361};
RN   [1] {ECO:0000313|EMBL:OWQ98983.1, ECO:0000313|Proteomes:UP000197361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22271 {ECO:0000313|EMBL:OWQ98983.1,
RC   ECO:0000313|Proteomes:UP000197361};
RX   PubMed=20023054; DOI=10.1099/ijs.0.018218-0;
RA   Zhang D.C., Liu H.C., Xin Y.H., Zhou Y.G., Schinner F., Margesin R.;
RT   "Sphingopyxis bauzanensis sp. nov., a psychrophilic bacterium isolated from
RT   soil.";
RL   Int. J. Syst. Evol. Microbiol. 60:2618-2622(2010).
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:OWQ98983.1}.
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DR   EMBL; NISK01000001; OWQ98983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246K0F9; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000197361; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd19410; HK9-like_sensor; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OWQ98983.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197361};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          218..269
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          274..346
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          348..400
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          418..635
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          636..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   657 AA;  73223 MW;  B92A863E31602A8D CRC64;
     MIDGGTRKTS RFWADRPLAV KGLVVVILPL AILLGSLVSL YLASSAETRA ENDVRRAFAI
     QRDTYQVHAL LAEAAAGVRG YVLTGEERFL QSYRQAQDEV PATMARLDTA IEDPVVRGHF
     ETLRLRERDK QDGLKQIVSL AERGTEVSSE VEDALIANKL ALDEVRRCID DIQRREAIVL
     DERRARVDEV RRGFLVVTGV SALVGLLGSL SAVYLFSTGI VRRVRKLEAD AQALAEGQRL
     TDRPEETDEI GRLAQRLVRA SALLHAREHD LRTSEERFRL VIERVRDYGI FALDPDGNVT
     SWNLGAERIK GWRAEDILGR HFSRFYPPDT RDHLPAEMLE RARQSGSAED EGWRVRKDGT
     RFWANVVITA LRDEQGELQG FAKVTRDMSE RRRSEDALRT AREEAEAASL AKSQFLSRTS
     HELRTPLNAI LGFGQLLEID EENFQGNHRE AIGQITKAGR HLLSLINDLL DISSIEAGGS
     DLKLNRIEMN ELLDEVHALA FPIVASAGLS YELEQAEQPA FVRADSRRVT QVILNLVGNA
     AKYNRGGTFV RLACISGDDF VKITVEDDGP GIPAEVAERL FTPFDRLGQQ DRAKIEGTGL
     GLALSKSLIE SMGGEIGYEP LPRGSRFWFK LPRPVAEDDT PADDLSPLTE ETSCQLD
//
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