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Database: UniProt
Entry: A0A1M3HFU9_9SPHI
LinkDB: A0A1M3HFU9_9SPHI
Original site: A0A1M3HFU9_9SPHI 
ID   A0A1M3HFU9_9SPHI        Unreviewed;       790 AA.
AC   A0A1M3HFU9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BGO55_13815 {ECO:0000313|EMBL:OJW57372.1};
OS   Sphingobacteriales bacterium 50-39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW57372.1, ECO:0000313|Proteomes:UP000184242};
RN   [1] {ECO:0000313|EMBL:OJW57372.1, ECO:0000313|Proteomes:UP000184242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=50-39 {ECO:0000313|EMBL:OJW57372.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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   -!- 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:OJW57372.1}.
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DR   EMBL; MKTZ01000011; OJW57372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3HFU9; -.
DR   STRING; 1895841.BGO55_13815; -.
DR   Proteomes; UP000184242; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        204..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        230..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        352..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          426..647
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          672..786
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         721
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   790 AA;  88878 MW;  3BB51118A743FE79 CRC64;
     MVVALRKIGW TLLTSLICLT CFAHREPDHD AQKGVLDLRN ADLFDHPVKL HGEWKFYWMH
     LLSPDNLTSA TPDVAPYPRL WKDLSLHGRK YPTQGYATYS LTVLLPKRRP RIGLEVPDTY
     CSYKLFVNGA VQSQNGQPDT TRDASTPFWA TRTVVLPAGE TDTLRVVIQI ANFWHAKGGP
     YKEILLGNKD DLILKKYQDA AYDFTLAGCL FMGGLFFLGL FIFGRHDKTT LYFSLFCLIY
     SYRMVGTDTY TLHLLFSDLS WFVTIRIEYL SLSLSVALFS LYTRHLYPND THPTFMKGMI
     WFCHLYTAII ILTPPTIFTR FMTTFLVVMF FCIAYAMYVY IRAARHKRSG SLFALLSTAV
     MLFVFLLLNL HFFGFIPPLR PVIFTGYISF FFLQSLSLSH RFAHTFKQAA FQAQQGLRAK
     SEFLSTMSHE IRTPLNAVIG MTHLLLRNEP RADQKEDLGV LLFSANNLLS IVNNILDYNK
     IEEGKIGFEQ IPMDLPAIAR NIVAGLQNAA GEKGISLLLE VDERLDRKLV GDPTRTSQVI
     NNLVHNAVKF TKEGSVRLII HVETLTRDAA TVLVKVVDTG IGIAREKQSM IFDRFTQADS
     STSRSYGGTG LGLAITKRIL ELQGVVLQLK SEPGKGSEFY FTQTFSFSNE AIGERTVSSN
     YTFRDQLLKG ITILLVEDNP LNVLVAQTML ENCGATVDVA TNGLEALDKL DASRHRLVLM
     DLHMPEMDGY EATILLRKRG ETLPIIALTA STPKEVESEA YAAGLTDVIV KPFDPDDLYR
     VILQHAGPAA
//
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