ID A0A1I4F1E6_9BACL Unreviewed; 588 AA.
AC A0A1I4F1E6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN03159341_103317 {ECO:0000313|EMBL:SFL11788.1};
OS Paenibacillus sp. 1_12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFL11788.1, ECO:0000313|Proteomes:UP000198699};
RN [1] {ECO:0000313|EMBL:SFL11788.1, ECO:0000313|Proteomes:UP000198699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_12 {ECO:0000313|EMBL:SFL11788.1,
RC ECO:0000313|Proteomes:UP000198699};
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOTE01000003; SFL11788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4F1E6; -.
DR STRING; 1566278.SAMN03159341_103317; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000198699; 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 CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR033479; dCache_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; PTHR42713; HISTIDINE KINASE-RELATED; 1.
DR PANTHER; PTHR42713:SF2; TWO-COMPONENT SENSOR KINASE YESM; 1.
DR Pfam; PF02743; dCache_1; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:SFL11788.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW 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 301..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 322..374
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 481..588
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 588 AA; 66693 MW; C5AFCBCE097B5D1D CRC64;
MLRKLGFVFF HYKSIQSTMA VAFSCLILFT TFCIAYTTYT LSTNAAEKSS REHTSQLIDQ
VNTNIETYLT YMENISQMVL SNSDIRQYLV NKTLSSTDGN AQLEQRISSQ LSSVLSTRKD
ISSILIFDNN GGIIPYNHMK LNPFAGPTQQ SWFLKAIEGN GNVVISAPHV QNIIQEYNWV
VSLSRQLSDV DGNRLGVMLV DLNYSVINDL CNKIELGKKG YIFILDQEGN IVYHPQQQLI
YSNLKQENID QVMSSQTSNF TTSEGKDSRM YTINQSKKGW KIVGVAYVDE LVPNKKEIQT
YILMWGIGLI AVAIFISIFL SSRISRPIKN LETSMKEVEK GNFDIQVPIE SRNEIGQLSK
RFNRMTAEIK ELMVQNVTEQ ELKRKSELKA LQAQINPHFL YNTLDSIIWM AEGKKSEEVV
LMVSALAKLF RLSISKGQEL ITIANEIEHI KSYLTIQKMR YKDKLDFQIA VDPQILSYKV
LKIILQPLVE NSIYHGIKHQ AGTGTILITG EIIAHRIRLQ VIDHGIGMSP EMVQRMLEKK
ENSGDGSGIG VSNVNQRIQL YYGTEYGITF ESEWGQGTTA NIWLPILE
//
