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Database: UniProt
Entry: Q71N01_PAEPP
LinkDB: Q71N01_PAEPP
Original site: Q71N01_PAEPP 
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
//
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