ID A0A1S2LJG3_9BACI Unreviewed; 425 AA.
AC A0A1S2LJG3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BKP37_13845 {ECO:0000313|EMBL:OIJ12506.1};
OS Anaerobacillus alkalilacustris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=393763 {ECO:0000313|EMBL:OIJ12506.1, ECO:0000313|Proteomes:UP000179524};
RN [1] {ECO:0000313|EMBL:OIJ12506.1, ECO:0000313|Proteomes:UP000179524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18345 {ECO:0000313|EMBL:OIJ12506.1,
RC ECO:0000313|Proteomes:UP000179524};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-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 -!- 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:OIJ12506.1}.
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DR EMBL; MLQR01000031; OIJ12506.1; -; Genomic_DNA.
DR RefSeq; WP_071310184.1; NZ_MLQR01000031.1.
DR AlphaFoldDB; A0A1S2LJG3; -.
DR Proteomes; UP000179524; 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 GO; GO:0071555; P:cell wall organization; 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 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 InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 210..417
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 425 AA; 48162 MW; 58B7AD758D23679E CRC64;
MVNLLLNVLT ILIGVFIYYI FVFNKQVHDK YQKPLIGFVA IVSIVLCMIF PAENINDYLY
DLRVIPFIIG AIYGGRNVGG VLLVAFILSQ YILIGSGTGF YLTIFQGLLV MIFTHIVSPN
FKSYSIRKKH LIGLAFLLVS WTVNVLNHFF FMPHTLDYYF LSILIFHSVT LLLTYSLIIH
IIEYIRQNQK MQEEINEIEK LRVISELAAS VSHEVRNPLT VTKGFLQLLK DNEITYDKRK
EYLDYSLCEL DRAKAIITGY LTYAKPSNGN ALTSIEVSEE IDKVVQVLMP YALMRGVELS
VENIMEVYVI GDPQKFQQCI VNIVKNAIEA MNEGGKVIVN TKLKHQTLIL SIQDFGEGMS
KEEISLLGLP FYSTKETGTG LGIMVAYSII KSMGWKVDIK SRESVGTTFF LEIPLSNSNS
KSYIS
//
