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Database: UniProt
Entry: A0A1G6H926_9BACT
LinkDB: A0A1G6H926_9BACT
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ID   A0A1G6H926_9BACT        Unreviewed;      1057 AA.
AC   A0A1G6H926;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216323_100851 {ECO:0000313|EMBL:SDB90787.1};
OS   Williamwhitmania taraxaci.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Williamwhitmaniaceae;
OC   Williamwhitmania.
OX   NCBI_TaxID=1640674 {ECO:0000313|EMBL:SDB90787.1, ECO:0000313|Proteomes:UP000199452};
RN   [1] {ECO:0000313|EMBL:SDB90787.1, ECO:0000313|Proteomes:UP000199452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A7P-90m {ECO:0000313|EMBL:SDB90787.1,
RC   ECO:0000313|Proteomes:UP000199452};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
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};
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DR   EMBL; FMYP01000008; SDB90787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6H926; -.
DR   STRING; 1640674.SAMN05216323_100851; -.
DR   OrthoDB; 1090267at2; -.
DR   Proteomes; UP000199452; 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; 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; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR013783; Ig-like_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
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; PF07495; Y_Y_Y; 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; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SDB90787.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199452};
KW   Transferase {ECO:0000313|EMBL:SDB90787.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        752..774
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          838..1056
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          790..831
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1057 AA;  120609 MW;  B48A35C3CAC9361B CRC64;
     METRYFRLIL VFLIFPLISI AQEIGFPIIR NYTPKEYKNA PQVMGAIQDS SGVMYFGVGS
     PTIEYDGVTW QSIQNEKNTT AFDFSMDKNG KIFVAANEEF GYLTKDKEGN TTYQSLTQQI
     HDTTVKLGTV YSVKLTSKFA YFQTSDAIFQ YGFASDDLQI FQADLNGSFS GNFVFQNIYY
     AQCDNKGLMK IENGVLKPAP QSAFFKNKNI FDIALSYDTT AMLILTRTNG QFLYQPLKDT
     IPQRNSILHK DFIRNNAISV GSPLGSNCFV LGSLNKGAFL VDKQGTILQQ YNESNQLQNN
     HVRGIAVDNT QNLWIGLSIG ISKTEPILDL SYWDKKAGLE DIVESVIRYN GTIYIATHAN
     VYYIGKDNKI YKVQNIPIGI NWCLFETKNI KSLLVGTTAG IYEIKGDKAQ PIYKGSRTTE
     IYQSIKNPNR ILSTSGDFFI SLIYRNGKWI YEGQWSGIKD NIRGIIEDNT GVVWLGTFRS
     GIIQVTPNFN NITKPQKIKY YDKKDGLVSL KNVLPFRFKN KIIWGSETGL TIYNSQTNRF
     DPFTEFGEQF CNGSRDVFSL QEMPDGKIWI CPLENRNADI GYLQPNQRGG YDWVYAPFRR
     ITDMFLVAFY IEPSGIAWIG GSEGLYRYDM SKDVKNYAQK FNCLIRRITV GTDSLIHIGT
     ISKTEPLKLA YDYNSLKFEF AAPFFDQEEK TLYSYQLIGF DKKWSKWSRQ TDKEYTNLGE
     GTYTFQVKAL NIYNVESKTS TFQLTILPPF YYTWWALTLY ILLSGLLIFL FIQWRIATLK
     RQKKYLKLKI REKTALVMQQ KEELQVTNEE LETINEALTE HRNELEIANA TKDKFFSIIA
     HDLRNPFNAL LGISELLVEK IKDRDFESSY KFAQAIHKAS SASFELLENL LNWSRSQTGK
     ISFTPEKLDV KDLIDSNIFL MNNSAESKGI HLTSTLSASV IAFADKNMVL TILRNLLTNA
     IKFSRKDDRI IVEVEETNEG VTIHVSDTGV GMNEETVGKI FKPGEKIKTV GTAKEPGTGL
     GLILCKEFVH WHHGKIWVES KEDVGSRFSF TLPKKRE
//
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