ID A0A0A8UWP6_LEGHA Unreviewed; 798 AA.
AC A0A0A8UWP6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LHA_2140 {ECO:0000313|EMBL:CEK11164.1};
OS Legionella hackeliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=449 {ECO:0000313|EMBL:CEK11164.1, ECO:0000313|Proteomes:UP000032803};
RN [1] {ECO:0000313|Proteomes:UP000032803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC35250 {ECO:0000313|Proteomes:UP000032803};
RA Gomez-Valero L.;
RL Submitted (SEP-2014) 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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; LN681225; CEK11164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8UWP6; -.
DR STRING; 449.LHA_2140; -.
DR KEGG; lha:LHA_2140; -.
DR PATRIC; fig|449.7.peg.318; -.
DR HOGENOM; CLU_000445_114_15_6; -.
DR Proteomes; UP000032803; Chromosome I.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:CEK11164.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:CEK11164.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 130..171
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 202..256
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 274..495
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 537..655
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 701..798
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 586
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 740
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 798 AA; 90251 MW; 7BE313C33AB6500E CRC64;
MANNALSLSS QAINEKLDSL FFLSSLQKTE KIVFFIDTQH KIEQIILKTN QPYFTGLSIY
SKKPFTEALT YMGLDANDIP DLIKKAKTTL FEHSEFHDKN LSHEYMLSIA YTGSNYVVIF
TLIDRKNEAL KAYINTIINT LPGAIYWKDK EGRYMGCNQS VANMAGFDHP EHVIGKTDFD
LCWKEFAQDW RNLDLDVMRE NKTYKREEIA KLADGRIITE LTIKSPLYNE KKEIVGVIGT
SMDITEQKNL EQDLIAARQK AEAASLAKTE FLENMRHDIR TPLTGIVGFA DILKMEADSP
HIKEYAENLI ASSHALLDLL DEVLEAIRVS SGEIPKLKKK FSLYKTLENI IKLNRAKAAH
KNLDLSLDID TNIPAYVIGD KVRVHRIILE LIANALNFTD FGFVKLSAHL AKRNNRELII
KLIVEDSGIG IPQDKQQEIY LQFKRLTPSY QGLYKGAGLG LSVVKQFIDE LEGEIYVKSA
PRKGSRFTCV IPLQEPLLDD DLGVDEELEK ALDAPYQTTY AEQIRSVQLD DSKKQYQVLV
VEDNPIAQSI ATSLLTSLNC NVDIAETGKK AIEQWKTNPY DLIFMDIGLP DLDGYEVTHL
IRVQELPKKT HTPIIALTAH VGEENKKRCI DAGMNAVINK PLTAKNCADI VATFIPGRKQ
EEMTQEIART SNLSEENANL FNLTEFPILD PEEGINTTGS EAMLAEMLTI MVNESLPNDL
ELMKKAHDEN DWGKTQQIAH KIKGGAVYVG TVKINIACQH LEQYWKTGQR ELLEKLYQQL
LRVINESIKE IKSWLASH
//
