ID A0A1H0BAM6_9BACL Unreviewed; 520 AA.
AC A0A1H0BAM6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04487897_102878 {ECO:0000313|EMBL:SDN42688.1};
OS Paenibacillus sp. yr247.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1761880 {ECO:0000313|EMBL:SDN42688.1, ECO:0000313|Proteomes:UP000198936};
RN [1] {ECO:0000313|EMBL:SDN42688.1, ECO:0000313|Proteomes:UP000198936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR247 {ECO:0000313|EMBL:SDN42688.1,
RC ECO:0000313|Proteomes:UP000198936};
RA de Groot N.N.;
RL Submitted (OCT-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};
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DR EMBL; FNIF01000002; SDN42688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0BAM6; -.
DR STRING; 1761880.SAMN04487897_102878; -.
DR Proteomes; UP000198936; Unassembled WGS sequence.
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 CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDN42688.1};
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:UP000198936};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 287..502
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 520 AA; 57284 MW; B62626891E07B1DA CRC64;
MMNKTDELVS WKSYLNTALF IALLTILLKA FDLYFDLVNI SLLYLFPVLF SAVRWGRGPS
FFAAGLGVLT FDFFFVPPTL SLTVADLRYI LSFIVFLSVA ALTASLASKL RSQFHQAQQK
EASTAALYAL SRKITAISDL DVLLIQIVQH VSDTLDAKAA ILLPNQMGEQ QLEAYSKEGE
AWASDESHLS IAAWVYKHNT RAGRGTQTLR ESSDLHVPLA TDRQVHGVLT VHVGDRNMSD
MPELIRIIEA LSDLVAVAIS RVKLANEAKV AQLTAESEKL RTALLDSLSH ELRTPLATII
GSVTGLLEGE DVFSPEDRRE LLLTIREGST RMNRLVGNLL GMVRIESGMM RLNKEWCGIE
DVVGVALAQL RDSLQQRKVS IRLAPELPSI PLDEVLIEQV LINVISNAIK YSPEGSEIVI
EAGQNREMLE LTIKDEGTGI APSDFEMVFE KFYRGNLTKH IPGTGLGLAI CKSIVEAHGG
HIAATKNENR GTAISISLPL QFAEKDGNGH DNFRSENLNH
//
