ID A0A1T2X977_9BACL Unreviewed; 566 AA.
AC A0A1T2X977;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BVG16_18785 {ECO:0000313|EMBL:OPA76362.1};
OS Paenibacillus selenitireducens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1324314 {ECO:0000313|EMBL:OPA76362.1, ECO:0000313|Proteomes:UP000190188};
RN [1] {ECO:0000313|EMBL:OPA76362.1, ECO:0000313|Proteomes:UP000190188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES3-24 {ECO:0000313|EMBL:OPA76362.1,
RC ECO:0000313|Proteomes:UP000190188};
RA Xu D., Yao R., Zheng S.;
RT "Genome analysis of Paenibacillus selenitrireducens ES3-24.";
RL Submitted (JAN-2017) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OPA76362.1}.
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DR EMBL; MSZX01000007; OPA76362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T2X977; -.
DR STRING; 1324314.BVG16_18785; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000190188; Unassembled WGS sequence.
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 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; 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 SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 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:OPA76362.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000190188};
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..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 297..349
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 457..561
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 566 AA; 65398 MW; 32E697DF9A97E117 CRC64;
MKQTKKRNFK ESTRHLFRLY TVIPFAILIV LFLVFTLING RMNLTQKTTE AAQSISQSIA
AVHQQYYEEI NQLAVSPAVM NYVTTHLNSD KVYSEFYDFN NQQQVKSIFH IVATNGVFLA
SSAPPDTLYA NFAFSNLITR IDHRPNDTLT EMNSFRYSHD RDTCYTFGKA IVKDHQTLGY
IIFQLNEADI QKIIFEQNNE IAMITDEHNT IIATTNNVTK GVLNKFSPKL DNQGHVLLND
GTYYMYSKRI PDTSIQVITL NSYKSEQYTY YTVSIFVLAA SVLLWIMIRI LSNKMSTRNS
ESIDKLIHAL AQLREGNFNG YVDIQTDDEF EILGDEYNVM LDRLKHLVEK NKELSALSTI
IEVKQLQSQF HPHFIFNVLE TLRYAIKIDA NQAQDIVMIL SRLLRYSIGH DRSVKLKDDM
NYVRDYLKLQ HIRFNERLEY RISVAEETHE VYVPKLLLQP LIENAIKYGY QNQSNVRIEI
RIYTSGGKLI LEVRDNGQGI NEETLENVNH ILQSQSNTTP HIGLYNVHRR LVLLYGEESG
VHIDSAQGEG TCVTLTIPYE WSDDHV
//