ID A0A089KYH2_9BACL Unreviewed; 578 AA.
AC A0A089KYH2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=R70331_19840 {ECO:0000313|EMBL:AIQ53552.1};
OS Paenibacillus sp. FSL R7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ53552.1, ECO:0000313|Proteomes:UP000029487};
RN [1] {ECO:0000313|EMBL:AIQ53552.1, ECO:0000313|Proteomes:UP000029487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ53552.1,
RC ECO:0000313|Proteomes:UP000029487};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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};
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DR EMBL; CP009284; AIQ53552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A089KYH2; -.
DR STRING; 1536773.R70331_19840; -.
DR KEGG; paee:R70331_19840; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_6_0_9; -.
DR Proteomes; UP000029487; Chromosome.
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 Gene3D; 6.10.340.10; -; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029487};
KW 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 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 470..572
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 348..375
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 578 AA; 65253 MW; 6AB878DA2240040B CRC64;
MKKGSFAPAV KSLRRTLVIY LLVGTLLPLL IVGIVSYTSI YSILSGKIGS GISASLRQEA
LSLENAIDNL DFASKQFALD GQIVEEMSSF LQEKQIYRKS QIMNSINQKI NLVNFTNPYI
GLTAYVMPGG KDPVLFTNMS MRRGFDTGNL PAFMRYNGAD YFGPHGTMYA VGDNVVFSEQ
RIVRVSGQHE LYIYLETNYS LLRKIFNEQA YGMAVNHLLV NQAGTSTYAI DGEVPDKILT
AAGLSGRPAH EELEGYHLFR YESPQGWKLV AAVKKSVFNS EIYAWFYKMI LLALSTLLFA
GLLAWLIWRR IYGPLRKVNV EIIRMAENVT APVAFTNVEE FDFVLSNFQQ MKDQVNELIQ
AVARNEKQKS QFEIEKLLSQ INPHFLHNTL NTVQWLARLN GQKEIDRLVT LLVKVLHYNL
GKQSLIVTIR EEIEAIRNYM ELQRIRYDYE FEFNVQAADG VLDAAVPRFL LQPLVENSIY
HGLSDHGRVD VIIVAHGDEE IQLCVRDNGA GMNDAQIAEL LSDDSAKKRG LGIGFAYVMR
MLRTYYGGQM DLQIKSGVGE GTDISIIIPR KSKEDFDD
//
