ID A0A1R0ZWI6_9BACL Unreviewed; 601 AA.
AC A0A1R0ZWI6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BK120_25475 {ECO:0000313|EMBL:OME77629.1};
OS Paenibacillus sp. FSL A5-0031.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920420 {ECO:0000313|EMBL:OME77629.1, ECO:0000313|Proteomes:UP000187447};
RN [1] {ECO:0000313|EMBL:OME77629.1, ECO:0000313|Proteomes:UP000187447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0031 {ECO:0000313|EMBL:OME77629.1,
RC ECO:0000313|Proteomes:UP000187447};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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:OME77629.1}.
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; MRTD01000017; OME77629.1; -; Genomic_DNA.
DR RefSeq; WP_076270318.1; NZ_MRTD01000017.1.
DR AlphaFoldDB; A0A1R0ZWI6; -.
DR Proteomes; UP000187447; 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; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; 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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 16..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 313..365
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 481..594
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 353..380
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 601 AA; 68862 MW; 4A3E8F8B25A2254C CRC64;
MYKRIIAYTL KYRLSYLMIV TNICIAVLPI ILLGTIGYFG YIKVMKENAL ENMEQFVVQT
NNRFDEYFNR VDQLSKSIFY NRGIQQITVA NKSWQESDAL LKNLNSFMSI DPTIKSIGLV
NAEDLRVIST GQLIGAKELE YIYTKNYQKA ITTKIQISPP LDGSDKKKGL LAYRQIKSIN
ENRYLQEIYI GIMLLDTQWI QQILQTGNLG NKANLYIVNE VGDLIGSSTN QLDFAKIQTL
IKDRPDNSVS DIRLNKVNYL YQSIPIKSLN WKFVALINKD KLLEKATDIQ YLVIAFVAIM
ILIVVWIAAV FNFRLTHPIT RLVDAFDWAA SGDLDAKLKF TYKNEITVIQ DHFNNMLNQI
KKLTENLLQS QQQLHQTEMD KQLFQLNGLQ SQINAHFLYN VLHSIRGMSL SNAKKEVAMA
IDNLVSYFRY ITRTDEYVLL NKELEHLERY IAIQKIRFGD RLQFKVAMDP SLNIHSIVKL
ILQPLVENSL VHGLEEKSGR WIIQIRAIVE DDRLRIKVMD NGAGMDEEKL AGLRAELAGL
SSSVTKDNNS IGQGIGLVNI HKRIQIYYGE PYGLSIKSWK DTGTIVTITV PLRTKEATRN
V
//