ID Q2K5H4_RHIEC Unreviewed; 1133 AA.
AC Q2K5H4;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=RHE_CH03146 {ECO:0000313|EMBL:ABC91912.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC91912.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC91912.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000133; ABC91912.1; -; Genomic_DNA.
DR RefSeq; WP_011426382.1; NC_007761.1.
DR AlphaFoldDB; Q2K5H4; -.
DR KEGG; ret:RHE_CH03146; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_12_0_5; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000001936; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 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; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABC91912.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW Transferase {ECO:0000313|EMBL:ABC91912.1}.
FT DOMAIN 192..262
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 601..822
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 840..961
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1003..1121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 894
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1052
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1133 AA; 125601 MW; C191721CB937B652 CRC64;
MKSAGDILEL ACRRIADLNT PAYVKNSELR YVAVNEAYAA FLGREISDFI GRRSRELFDR
PEEEDREDKE RRALVFGTEE NAICFDAANL AHERIQIESF SPSPDRIYVL GMFEPRERRA
AGNEANGGSS RTVNDSGVAA DFARVREALE KLDHPIGIFA ADGRPLVVNA AYRKGARPAP
AHGSAWGKSV NELDALRTVL EDLPVAVFVR DDKHRLIYAN KYYETFSGRA RSEYLGMTEH
EMFGPEGAEP IYQENLLALR DGISVELESE MPSTSGHVYP VISRVNRVIT ADGRTYVVGS
FSDISPLKER EKALIASRKQ EEVLHRDIES ILRSLPIGVL ILDNDHRILY VNDEFYSIWE
LPREDRFDGR PFIDVIRRNH ELGRYDGTRT PEELYAFRKH LFEAEEPEPI EVGWAGGKSV
IFDSRRISND RILLTYADIS AVREREKEIH ETRAALERVG EMMRDATHAM SQGLAIVQDG
IIKMSNDAMA DILQIPPHYI EAGQGWLGMF EFCAARGDFH DAADEILQGW RANIAARQPI
STVFHVGGER WVNMEATVSS GQHWVALFTD VTELKSREEE LRQLLSRAEA ADRAKSEFLA
NMSHEIRTPM NGVLGMAELL AKTNLDTRQK TFIDIIVKSG NALLTIINDI LDFSKIDAGQ
MKLRKAAFDL VEAVEDVATL LSSHAAEKNI ELLVRAAPDL PAAVIGDAGR FRQIVTNLVG
NAVKFTERGH VFVDVGFQAA AGGEIIASIR IEDTGIGIPR EKLDSVFEKF SQVDASSTRR
HEGTGLGLAI TAGLVDLFGG YINAESEWGR GSVFTVNLPF AVAAARLEPK PLPINVQGAR
ILVVDDNEVN RRILTEQLSL WGFDGVAAEG GGTGLAILEA AADLGVTVDA VVLDYHMPDM
NGANVARRLR ADPRFVDLPI IFLTSMDISG TEKEFAALNG QAHLMKPARA NVLRNTVVEV
VRARRVKQAS EAEIARLQTE AAVPAPEPAP MLVPQKRADE FVDVLVAEDN EVNQIVFTQI
LQSSGLSFLV VKNGEEAVAA WESHTPRIIM MDVSMPVMNG HEATRTIRER EKGQGHRVPI
IGVTAHALES DRELCLDAGM DDYMSKPISP ELLEEKIRQW LGKDEQQPGR TSS
//
