ID A0A011AMK1_9BACL Unreviewed; 558 AA.
AC A0A011AMK1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SacsacDRAFT_0166 {ECO:0000313|EMBL:EXG83201.1};
OS Saccharibacillus sacchari DSM 19268.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Saccharibacillus.
OX NCBI_TaxID=915437 {ECO:0000313|EMBL:EXG83201.1, ECO:0000313|Proteomes:UP000053380};
RN [1] {ECO:0000313|EMBL:EXG83201.1, ECO:0000313|Proteomes:UP000053380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19268 {ECO:0000313|EMBL:EXG83201.1,
RC ECO:0000313|Proteomes:UP000053380};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:EXG83201.1}.
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DR EMBL; JFBU01000001; EXG83201.1; -; Genomic_DNA.
DR RefSeq; WP_051506757.1; NZ_KK073875.1.
DR AlphaFoldDB; A0A011AMK1; -.
DR PATRIC; fig|915437.3.peg.168; -.
DR HOGENOM; CLU_000445_104_15_9; -.
DR Proteomes; UP000053380; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EXG83201.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000053380};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 78..295
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 320..440
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 464..557
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 44..71
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 370
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 503
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 558 AA; 61882 MW; 4E054ADBE0C9EF64 CRC64;
MEVEDKNEIQ RLHAIIEKLN DRIVRGQMKE EKILNEFSSM NNELVTLQRQ LAKSNGELEK
AVREAQRAND SKSRFLAMIS HEFRTPMNGI LGMTELLRES PLAAEQRGWT DLIEESASEL
LGMVNDLLDL SKSDAGALTI EEKPFDLRLV VEHVVQLLQP KAESKRNTIK AEFDPSIAGM
LSGDPTRIRQ ILINLINNAN TFTESGTIQV AVYPLPGYRG KVRFEVRDSG IGISQANIDT
LFKPYAQTQA GKAKEGTGLG LMICKSLVKS MKGEIGVFSR EDTGSTFWFE LHLPEADEPK
ESGTVLYAVS DQVPIAANMN ILVAEDNAVN GRVIRMQLKK LGLESVDVAE NGEAAVAAFR
SGSYGLVFMD KQMPVMDGTE AARAIREFER DEMRRAVPIV ALTGEATESE RAACFAAGMN
DFLSKPINVE TLKAVLQKWM PKNSRQALDP DVVRELIELD EGNDPEIFRS LLEVYEEETP
AKLLQLEEAV LSGNLEQAMR TAHSLKSGSL SLGVHYFSEL LEQIEQRLKA GRAEQAKDML
PVLNGAYEAA CAELHRFA
//
