ID A0A261QHI7_9BACI Unreviewed; 499 AA.
AC A0A261QHI7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CEW92_07425 {ECO:0000313|EMBL:OZI12296.1};
OS Bacillaceae bacterium SAS-127.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=2015203 {ECO:0000313|EMBL:OZI12296.1, ECO:0000313|Proteomes:UP000217062};
RN [1] {ECO:0000313|EMBL:OZI12296.1, ECO:0000313|Proteomes:UP000217062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAS-127 {ECO:0000313|EMBL:OZI12296.1,
RC ECO:0000313|Proteomes:UP000217062};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Indiibacillus sp. (SAS-127) genome sequencing.";
RL Submitted (JUN-2017) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OZI12296.1}.
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DR EMBL; NKXN01000030; OZI12296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261QHI7; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000217062; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd18773; PDC1_HK_sensor; 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; 2.
DR InterPro; IPR033479; dCache_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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF55; SPORULATION KINASE D; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OZI12296.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000217062};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 289..495
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 499 AA; 56977 MW; 3AF8C69E2EDE1D41 CRC64;
MKKHGKFLYI FVVILPSILA IIGFYDLLSN RAGQQHNKEL EWIASLHKNQ MDQFISETTI
SLDILAVSIE EDLNNLDKVQ SIFKKMANQD PRYGGIYLLD FEGNLLVGTN DYLKQYNLRD
KQYIKEVLLT KDTAVSDEVE TLSNNQAVIA VATPVLKSEQ QVEAIIVSHI RLDYMKNIMR
VLTPEHSIFF ENAKQIPVFS VNERPEASKN ELSLKYPLSQ LPWNLVITTD EQKNNNFIGY
TFLFAVVFIV IVHIIYLFIK YMMLKRQTNL ERMQQETQKL ELIGTLAAST AHEIRNPLTG
IKGLVQLLNE KYNDQEDEFY FSVINKEVAR INQIVSELLI LGKPTAQKVS IVDMKDIISD
LNPLIYSEAN LYSVDYKFTL PEQEIWVKVN IDQMKQVILN LTKNAFEAMN NGGELRLTVL
KRENSCQLSI TDNGPGIEKE KHDQLFKPFF TSKEDGTGLG LVVCKRIIDS FDGTIEIESE
FGFGTTVTIS IPLQTPANE
//
