ID A0A0E3WH10_9BACL Unreviewed; 536 AA.
AC A0A0E3WH10;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, 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=PRIO_2064 {ECO:0000313|EMBL:CQR54473.1};
OS Paenibacillus riograndensis SBR5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC Paenibacillus sonchi group.
OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR54473.1, ECO:0000313|Proteomes:UP000033163};
RN [1] {ECO:0000313|Proteomes:UP000033163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (MAR-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN831776; CQR54473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3WH10; -.
DR STRING; 483937.AMQ84_02850; -.
DR KEGG; pri:PRIO_2064; -.
DR PATRIC; fig|1073571.4.peg.2175; -.
DR HOGENOM; CLU_020211_11_2_9; -.
DR Proteomes; UP000033163; Chromosome I.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 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:0000313|EMBL:CQR54473.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..528
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 536 AA; 59150 MW; 64A2B715DF6F0870 CRC64;
MVKTKDYGLR TKVTIMVSAV VMLVMLVLYI IFRNQIIPQT RHALEDKATA IARTIALIPL
VSEGLNEGRS KEIQAYTSKI TRRNDIMFVV VIDMHSIRYS HPDPSRIGKP FVGGGQKAAL
HGEESISEGE GLLGKSLRAF VPVYNNRGSQ VGVVVVGLSM ERVHLLIRQN EWTIIAILLS
GAVLGAAGAM VLARKIKQMM FGMEPADISK LLQERSAMLQ STREGIIAVD HAARISMINR
EAERLLGTAG ITGNGMTRHI ADYWPELRLE QVLSSGESRQ DQELELNGIT LLVSSVPIQV
NGRIAGAIAT FRDKTELAVL AERLSGISVY ADALRAGAHE YMNKLHVIMG MTHMGLFDEL
QEYISGTVSN YQNEIGSITR QIKDPVMAGF LLGKLSRARE AGIELQLAED SYLPESADPQ
VIHQLITIVG NLLDNAMEVL EGQHMKEIEL SFQYERGRLI CTVRDNGPGI PEPLREQIFV
QGFSTKGEQR GMGLYLVRKS VEKLQGQLKM IPGREPGTIF MADVPYAVKG DETNDH
//
