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Database: UniProt
Entry: A0A495RX54_SPHMI
LinkDB: A0A495RX54_SPHMI
Original site: A0A495RX54_SPHMI 
ID   A0A495RX54_SPHMI        Unreviewed;       486 AA.
AC   A0A495RX54;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DFR51_1494 {ECO:0000313|EMBL:RKS91920.1};
OS   Sphingosinicella microcystinivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingosinicellaceae; Sphingosinicella.
OX   NCBI_TaxID=335406 {ECO:0000313|EMBL:RKS91920.1, ECO:0000313|Proteomes:UP000276029};
RN   [1] {ECO:0000313|EMBL:RKS91920.1, ECO:0000313|Proteomes:UP000276029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19791 {ECO:0000313|EMBL:RKS91920.1,
RC   ECO:0000313|Proteomes:UP000276029};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (OCT-2018) 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   -!- 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:RKS91920.1}.
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DR   EMBL; RBWX01000007; RKS91920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495RX54; -.
DR   OrthoDB; 7933832at2; -.
DR   Proteomes; UP000276029; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          265..486
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   486 AA;  52038 MW;  6412EDE54738BCEE CRC64;
     MFEPRDIRPG HASAFDVLAA ADPALAGAVV FECSSTGALF EANAAYTELE RAAMLTPGEL
     ASRLVAALAP AGESVSASFT LELLSEPRHF HIRFVPVSTQ ARNELKFVGI MRESSTTVGE
     RERETLAGWQ GDELVRVNSD WYWETDSRGS LTSISRALEL LVGQPAGALL GRPLTAIGTL
     LRGENGEVPY ETAQARGSSF RDQLMSVTTQ GGATRLYRLA GVAVPTKDGG CGYRGVAAVV
     PDSARLIERM RTELGRTAKA NFLSSMSHEL RTPLNAIIGF AEAMNHEVHG PLKAQYVEYA
     GDIANAGRHL LGLIQDLLDI SSLDSGEIDL DTEDFDLAAL IEQARAMVQM KASARNIDIK
     AVALDAPLRA RGDRRRTLQI LVNLLTNAVK FTPEGGFVGA EPATSLPGYV AVTVWDSGPG
     IAPEDQARVF EKFEQLPTPP YVASGEGTGL GLHISRRLAE LMNGGLTLES HKGMGARFTL
     TLPVSD
//
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