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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//