ID A0A0Q9TFS9_9BACL Unreviewed; 960 AA.
AC A0A0Q9TFS9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG93_24310 {ECO:0000313|EMBL:KRF38603.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF38603.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF38603.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF38603.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF38603.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF38603.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRF38603.1}.
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DR EMBL; LMSP01000007; KRF38603.1; -; Genomic_DNA.
DR RefSeq; WP_056831280.1; NZ_LMSP01000007.1.
DR AlphaFoldDB; A0A0Q9TFS9; -.
DR STRING; 1736411.ASG93_24310; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF55781; GAF domain-like; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 572..786
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 793..910
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 226..253
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 845
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 960 AA; 109599 MW; E0DFD8424D2A71F8 CRC64;
MKSFMRSRIS MLYVILIVVL LVFVSVSNFI ASRNMENESD AIVHDSIPIS NTTNSLLTDL
INQETGIRGF EISGNEQYLE PYTSGKKQLE LDLNTISQYD KKYPTLQLIM DTQAIPAINN
LQKFFDTHLE LVRAGKTEES KARIASGKTM MDRYRVVHVS IEKTIDQITS DAYTASLHAG
KTSRTITMVG SIIALIAGGM SIFISYRAYH AEEEIRRSEE TYRYMAESLE TQNEEIMAQQ
EEQQITLAKL SEREMDLELI SSYQEKLTGY VKLKDFLKHT LPALLNSLSQ DAALVVMERH
AEDSTSYEVI HSIGYPKEHI NLNQRELFGP AMRVFDEGTP IVHTRDISGH EQGVHGGMTR
AVDQYVPLMD DKQKVIGFLL LTNYQSSIFQ ENNERLTKGL VRQFGLAFYA QVMNDERLRQ
AASLAELNDQ LITEKQLIEG QRDLIQNILE SAHEGMMMCD SQGTILFSNH RMSRYFSLNE
RIGENLVDSC HEIAADSPSF IGVASSIEAL IDGSLSNLTQ RFSFELEDQV QHAELYATVV
GEDTEQQGYL FVFRDRTEEE RIDEMKNEFI SIVSHELRTP LASVLGFIEI LLHRELSQEK
QKKYMETINK EAHRLSNLIN DFLDLQRMES GRQLYHFSPV NLLPTLQEIA EQWQDKHSHR
ILIHQQEAEL YVRADADRIR QVFDNLISNA IKYSPEADHI DIHLTVDQGK INIAIQDYGL
GIPEEARDQM FTKFFRVDNS DRRQIGGTGL GLAIVKEIVE GHGGHISYTS EMRQGTTFRI
EFDQYEISNM DGQIVIFEDD DNLAKLIQVA LNKLGLPSMQ LRSAEEGIIA LNRCKGEGPI
LFIVDIHLEG AKTGWDFIAD LYRHPVHYQT PVIVSTALDP PHDYHEKEIE KYLKKPFTME
RLVQVAKRLL DNKQNNAYVF PAQNKEKLST TLQRNGIDVL GMKESMDMIE VEIKKPQSDA
//
