ID M8DBY3_9BACL Unreviewed; 404 AA.
AC M8DBY3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=I532_19971 {ECO:0000313|EMBL:EMT50918.1};
OS Brevibacillus borstelensis AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT50918.1, ECO:0000313|Proteomes:UP000012081};
RN [1] {ECO:0000313|EMBL:EMT50918.1, ECO:0000313|Proteomes:UP000012081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT50918.1,
RC ECO:0000313|Proteomes:UP000012081};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL Submitted (MAR-2013) 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:EMT50918.1}.
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DR EMBL; APBN01000011; EMT50918.1; -; Genomic_DNA.
DR AlphaFoldDB; M8DBY3; -.
DR STRING; 1300222.I532_19971; -.
DR PATRIC; fig|1300222.3.peg.4197; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000012081; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMT50918.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000012081};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 41..111
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 115..167
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 192..395
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 404 AA; 45930 MW; 7AE0FC8EE3FCE8EC CRC64;
MQRLAIMKTP GKSEEGSRKL LVTIEIWKER YSLKFGADVE NKSLFLQTFT YSSIGMALVS
LDGQWMKVNQ SFCDLIGYTE EELLSRTFQD ITHPDDLAAD LDYMQQLLEG KIESYQMRKR
YVLKQGRVVW VLLNVSMVRD DCGRPLYFLT QVQDITALKR SEGLLLENER KLTEELLRNS
EKLTIAGQLA AGIAHEIRNP LTSLKGFLQL IKKGPDYKTE YLDIMEAELD RIEVIVNELL
LLAKPTDRKF EEKDVKSMLQ NVITLLETQA LIHNVQILTA FTPGVTIYCD ENQMKQVFIN
LMKNAIEAMP GGGKLLIQVK KKQELAVIRF IDQGCGIPKE KLKQIGSPFY STKEDGNGLG
LMVSYNIIEN HHGKIHIESE IGVGSTFTVS LPIYTPSRLH PAFH
//
