ID A0A0W0XLB5_9GAMM Unreviewed; 538 AA.
AC A0A0W0XLB5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=fixL {ECO:0000313|EMBL:KTD45469.1};
GN ORFNames=Lqui_2940 {ECO:0000313|EMBL:KTD45469.1};
OS Legionella quinlivanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD45469.1, ECO:0000313|Proteomes:UP000054618};
RN [1] {ECO:0000313|EMBL:KTD45469.1, ECO:0000313|Proteomes:UP000054618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD45469.1,
RC ECO:0000313|Proteomes:UP000054618};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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 -!- 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:KTD45469.1}.
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DR EMBL; LNYS01000025; KTD45469.1; -; Genomic_DNA.
DR RefSeq; WP_058508991.1; NZ_UGOX01000001.1.
DR AlphaFoldDB; A0A0W0XLB5; -.
DR STRING; 45073.Lqui_2940; -.
DR PATRIC; fig|45073.5.peg.3118; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000054618; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KTD45469.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054618};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 281..538
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 538 AA; 60884 MW; BFF61549F712A3F9 CRC64;
MSIRNKILFS MLLVVFLFIP ANLFLLARYL DVKESFLIII ERTVPRLEAL LTMKNLVMQI
NFFMSYDEKF SQSLSKKDRE HLAVIKDEFL SILGELGEQQ TIYQKYESSS ADQNGRKLNQ
LRDTVVLAAL DLFLAGERQK SLSEITVKKG FLQIKEKDLN DFINRILVQE STLLEEERER
TIAASTALFN LLLILNGIII LITFGLSIFL ANIISKPIIK LSDFAGKIDY DHLAPMLPIM
TRDEIGELQS HLNEMVMKLD RAKTRLIETS RSAGVAEIAT SILHNVGNVL NSVNTSVAML
SEAAQHSYVV QLPKLLSILE ENQEHLDLYL KEDERGKLFI PYFKKLIEQL ENEQLQMSEE
LNQLNNNLTH VNQVIDMQQS SGQASSQIKE TIELEELIED ILLLYANRLR KASINVERQY
GNISPIISVR TKIQQIIINL IKNAIDALIL GEQQEKRLII KVETTSPSLA CITISDNGIG
IQKDDLTRIF SFGFTTKKEG HGYGLHNCAL LARELGGELR VQSKGSGQGS SFTLEIPY
//
