ID Q71N01_PAEPP Unreviewed; 346 AA.
AC Q71N01;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
OS Paenibacillus popilliae (Bacillus popilliae).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=78057 {ECO:0000313|EMBL:AAQ04069.1};
RN [1] {ECO:0000313|EMBL:AAQ04069.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bl 17 {ECO:0000313|EMBL:AAQ04069.1};
RX PubMed=15980329; DOI=10.1128/AAC.49.7.2625-2633.2005;
RA Fraimow H., Knob C., Herrero I.A., Patel R.;
RT "Putative VanRS-like two-component regulatory system associated with the
RT inducible glycopeptide resistance cluster of Paenibacillus popilliae.";
RL Antimicrob. Agents Chemother. 49:2625-2633(2005).
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}.
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DR EMBL; AF432144; AAQ04069.1; -; Genomic_DNA.
DR AlphaFoldDB; Q71N01; -.
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 CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR008358; Sig_transdc_His_kin/Pase_MprB.
DR PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF1; SENSOR HISTIDINE KINASE CPXA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR01780; LANTIREGPROT.
DR SMART; SM00304; HAMP; 1.
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; PS50885; HAMP; 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, ECO:0000313|EMBL:AAQ04069.1};
KW Membrane {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 42..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..114
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 129..345
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 346 AA; 39742 MW; CE0E39FFFBAEB073 CRC64;
MLLSSAITYL LFKVLQLYYY TSVDYGDTLA YFRKIIQNIG DFNVFLLLFI LLSILFFFLL
TKPYSAYFNE ISKGIHYLAQ GDFKHRVQIL SNDEFSDIAQ SINLASEKLE QAIERGDFSE
SSKEQLVVNL AHDLRTPLTS VLGYLDLILK DDNLTENQIR HYLTIAFTKS QRLERLIDEL
FEITRMNYGM LPIKKKQIDL SELLIQLKEE LYPVFEKNDL IARMNITSPL SIMGDGELLA
RVFENLLINA NRYGYEGQYV DIIGFIDSEE VVIQVINYGD AIPPDELPHI FDMLFTGDKA
RTHQENSTGL GLFIADNIVE QHNGTITAES DLIRTIFEVR LPMADS
//