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Database: UniProt
Entry: F6EZF1_SPHCR
LinkDB: F6EZF1_SPHCR
Original site: F6EZF1_SPHCR 
ID   F6EZF1_SPHCR            Unreviewed;       781 AA.
AC   F6EZF1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Sphch_0732 {ECO:0000313|EMBL:AEG48427.1};
OS   Sphingobium chlorophenolicum L-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG48427.1, ECO:0000313|Proteomes:UP000007150};
RN   [1] {ECO:0000313|EMBL:AEG48427.1, ECO:0000313|Proteomes:UP000007150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-1 {ECO:0000313|EMBL:AEG48427.1,
RC   ECO:0000313|Proteomes:UP000007150};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT   "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-1.";
RL   Submitted (MAY-2011) 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; CP002798; AEG48427.1; -; Genomic_DNA.
DR   RefSeq; WP_013846692.1; NC_015593.1.
DR   AlphaFoldDB; F6EZF1; -.
DR   STRING; 690566.Sphch_0732; -.
DR   KEGG; sch:Sphch_0732; -.
DR   HOGENOM; CLU_018130_0_0_5; -.
DR   Proteomes; UP000007150; Chromosome 1.
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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000014; PAS.
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   Pfam; PF12860; PAS_7; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 3.
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   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AEG48427.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:AEG48427.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          565..781
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          154..181
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          277..304
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   781 AA;  84930 MW;  7CF9CBC80EFAE865 CRC64;
     MTLTPLAAVI FGVVLAAWLG AAVWALSSGQ RRRREGMQAQ GKLDRLSVLL ASAPAAPIVV
     HPDGRLEAAD RLAKWLGKDR GPTFLSELTA PDGGLEADDA AALAQEIAAA QRAGRSFALA
     VRGVDSSRLL LVRGAPAGPV LAESGGVVLW IFDATDSQSE IQSLKGKVEQ LREALEAMAG
     LVEAAPFPMW HRTADMRLSL VNTAYVRAVD GESAREVIAH GTELVETVGG LTPQAAAAQT
     LTDGAPVERM VPATIDGERR TIRVVDVPLG AAGVAGFAMD QNELEQARVE HRRLEAAQRD
     LLDRLSAGVA RFGSDRALRF WNQPFMSLFG LDQERLSDNP PFERVLDQMR EARRLPENRD
     FPAWRAERRD WFLSPDPREE NWLLADGTHL RVYAQPLPDG GLLLIFEDRT EQVQLSSARD
     TLLRVRTATF DNLFESIGVF SSDGRLHLWN SRFRTIWDVS EDLLAQHPRI DELMRTVQSR
     LAKPQQGNLV RELVRAATVE RKQRVGHVGF ADGRIFEFAA IPLPDGNALF TMLDVTDSRR
     VEQVLRDRND ALEQADKVKT AFVTNMSYEL RTPLTTIAGF AEMMSAGYAG ELSTSAKEYV
     DGILQSTNRL SMLIDNVLDL TQGEAGMLPV EKAPVDLAAE ARDAVARIKG DATAKGIDLA
     LSLQASLGTI QGDKRRIGQA LDHLLENAVR YCSRGGRVLL HGDGTTDNAR LVVSDNGPGI
     DAKRQATIFD ASSRTEQARN GGKAGIGLPL ARQLAQAHGG TLQLVSEPGQ GTMVVIELPR
     G
//
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