ID A0A117N2J3_RHILI Unreviewed; 459 AA.
AC A0A117N2J3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AU467_28770 {ECO:0000313|EMBL:KUM24860.1};
OS Rhizobium loti (Mesorhizobium loti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=381 {ECO:0000313|EMBL:KUM24860.1, ECO:0000313|Proteomes:UP000053176};
RN [1] {ECO:0000313|EMBL:KUM24860.1, ECO:0000313|Proteomes:UP000053176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM24860.1,
RC ECO:0000313|Proteomes:UP000053176};
RA Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT efficient symbiont and plant-growth promoting strain isolated from Zn-
RT mining soil using Leucaena leucocephala as a trap plant.";
RL Submitted (DEC-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:KUM24860.1}.
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DR EMBL; LPWA01000128; KUM24860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117N2J3; -.
DR OrthoDB; 9815202at2; -.
DR Proteomes; UP000053176; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUM24860.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 16..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 179..232
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 240..455
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 459 AA; 49294 MW; A666309102E58CF5 CRC64;
MNEGRPSLLR STPFRLALTF AFLFVLAFIL SGAIVYQLMS NDLARRLDES IKETYSVVAV
TYAESDRDDL IATVNDHAQL DPDKDQLFSL TDTQGNRLAG NFTASGLPDG FSMFAARLPG
VPPDTMYRAY SGTVGNNNLT VAFSLSETEE LETIVLMSFG WGTLFITGLA IAGGALLASR
VQRRLDGIAA TMVDVSHGRL DARIPLIGNG DDIDAVSTQV NAALDRLSAL VDGMREVSAN
IAHDLKTPLN RLQMILEQAA DKTASSEDVS GELADARAES LQINQTFDAL LRIAQIEAGA
RKARFVDLDV SGIVNTIGEV YADVAEDDGK SLSTQLVPDA KWYIHGDRDL LMQMLANLVE
NALRHCPPGT AIELSVARES DRVLVHVRDN GPGIPADERE KVFQRLYRLD SSRTTPGSGL
GLSLVKAVAD LHGATIALED NNPGLVVIAS FPAGRSPGG
//
