ID A0A0W0ZNR7_9GAMM Unreviewed; 418 AA.
AC A0A0W0ZNR7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:KTD70879.1};
GN ORFNames=Ltuc_2890 {ECO:0000313|EMBL:KTD70879.1};
OS Legionella tucsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD70879.1, ECO:0000313|Proteomes:UP000054693};
RN [1] {ECO:0000313|EMBL:KTD70879.1, ECO:0000313|Proteomes:UP000054693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD70879.1,
RC ECO:0000313|Proteomes:UP000054693};
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:KTD70879.1}.
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DR EMBL; LNZA01000012; KTD70879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0ZNR7; -.
DR STRING; 40335.Ltuc_2890; -.
DR PATRIC; fig|40335.7.peg.3092; -.
DR Proteomes; UP000054693; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KTD70879.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054693};
KW Transferase {ECO:0000313|EMBL:KTD70879.1}.
FT DOMAIN 125..177
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 197..412
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 418 AA; 47722 MW; 6FA0CF10F28D3EBE CRC64;
MVLFSKVNEI VSSAETVANG GVMINSKVAL DLKKKGSKDL FSNNRTYEIS HEYLMELLDV
GKLNVWQWDL GTNEVIDFGY SESLSISNEK SEVGHIDHFI TRLHPEDREE IANTLVNSLT
HFEDHYSDFR ILSAKGHYEW VSARGRYIRD AENNPIKMIG TWHFITEQKH NQELIKLQQT
TLERISRCYF SGEAASSLSH EISQPLLALN SYLLGSILRL QQEDKETNEF ISVLQKALEQ
VELISTIIKR MKRFVTHGEL HFERVNLNLL AKQSVILSKF YSNFSGTVQY EFDEDLTEVY
LDRNQMRQVF LNLINNAFEA MFDAKTMNPI LLIKIKNYET YVLVTIIDNG PGVSQNVLDN
LFASCYSTKE YGLGLGLSIC KKIIEAHGGA IKIERNASGE GTVSSFRLPN QLLESRDE
//