ID I3E669_BACMT Unreviewed; 378 AA.
AC I3E669;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PB1_03595 {ECO:0000313|EMBL:EIJ81990.1};
OS Bacillus methanolicus PB1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=997296 {ECO:0000313|EMBL:EIJ81990.1, ECO:0000313|Proteomes:UP000010523};
RN [1] {ECO:0000313|EMBL:EIJ81990.1, ECO:0000313|Proteomes:UP000010523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1 {ECO:0000313|EMBL:EIJ81990.1,
RC ECO:0000313|Proteomes:UP000010523};
RX PubMed=22610424; DOI=10.1128/AEM.00703-12;
RA Heggeset T.M., Krog A., Balzer S., Wentzel A., Ellingsen T.E.,
RA Brautaset T.;
RT "Genome Sequence of Thermotolerant Bacillus methanolicus: Features and
RT Regulation Related to Methylotrophy and Production of L-Lysine and L-
RT Glutamate from Methanol.";
RL Appl. Environ. Microbiol. 78:5170-5181(2012).
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:EIJ81990.1}.
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DR EMBL; AFEU01000001; EIJ81990.1; -; Genomic_DNA.
DR RefSeq; WP_003350766.1; NZ_AFEU01000001.1.
DR AlphaFoldDB; I3E669; -.
DR STRING; 997296.PB1_03595; -.
DR PATRIC; fig|997296.3.peg.787; -.
DR eggNOG; COG4191; Bacteria.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000010523; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd14755; GS_BA2291-HK-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.490.70; Histidine kinase N-terminal domain; 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; IPR018984; Histidine_kinase_N.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF09385; HisK_N; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EIJ81990.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 166..374
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 378 AA; 43936 MW; 12DF7ADF4902A43A CRC64;
MLATTKKRLA DLLESNKKVM LDEWEKMIME SDKDPFKDHI KQNGEAIFNI VLSVFTRSEE
ELETYIKKLA YVVGDERVKA DINIGEFVYN VNIGRSIINK YLYKMDMDWT ELQMSIDNIN
YCFDKFLYYT VSYYTEAKNK IIEEKSKFID STHKDRLTLL GQMTSSFIHE FRNPLTSIQG
FIQLLKADYP SMNYLDIISN ELEQLNFRIS QFLLLSKKEL IGKEKNIFSL KSLVDEVLTF
LYPSILDCKV RIIKVVDDIK LYGYSDEIRQ VLINIVFNAI DVLSQYRSDP LIEIKGDFTN
EKKEFIKLEI ANNGPMIPKE LLQTIFEPFV TTKKLGTGLG LFVCKEIIEK HKGTLSCESN
KEKTVFTIIL PSAETTHI
//