ID Q2K1D9_RHIEC Unreviewed; 1968 AA. AC Q2K1D9; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN OrderedLocusNames=RHE_PC00094 {ECO:0000313|EMBL:ABC93301.1}; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OG Plasmid p42c {ECO:0000313|EMBL:ABC93301.1, OG ECO:0000313|Proteomes:UP000001936}. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC93301.1, ECO:0000313|Proteomes:UP000001936}; RN [1] {ECO:0000313|EMBL:ABC93301.1, 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; CP000136; ABC93301.1; -; Genomic_DNA. DR KEGG; ret:RHE_PC00094; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2203; Bacteria. DR eggNOG; COG3899; Bacteria. DR eggNOG; COG4191; Bacteria. DR HOGENOM; CLU_000445_34_2_5; -. DR Proteomes; UP000001936; Plasmid p42c. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR CDD; cd00082; HisKA; 1. DR CDD; cd00130; PAS; 2. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.450.40; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.30.450.20; PAS domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR041664; AAA_16. DR InterPro; IPR003018; GAF. DR InterPro; IPR029016; GAF-like_dom_sf. 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; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000014; PAS. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR NCBIfam; TIGR00229; sensory_box; 2. DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1. DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1. DR Pfam; PF13191; AAA_16; 1. DR Pfam; PF01590; GAF; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF13426; PAS_9; 2. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00065; GAF; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00091; PAS; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF55781; GAF domain-like; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50113; PAC; 2. DR PROSITE; PS50112; PAS; 2. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:ABC93301.1}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Plasmid {ECO:0000313|EMBL:ABC93301.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001936}; KW Transferase {ECO:0000313|EMBL:ABC93301.1}. FT DOMAIN 1..292 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1484..1540 FT /note="PAS" FT /evidence="ECO:0000259|PROSITE:PS50112" FT DOMAIN 1559..1608 FT /note="PAC" FT /evidence="ECO:0000259|PROSITE:PS50113" FT DOMAIN 1609..1653 FT /note="PAS" FT /evidence="ECO:0000259|PROSITE:PS50112" FT DOMAIN 1681..1731 FT /note="PAC" FT /evidence="ECO:0000259|PROSITE:PS50113" FT DOMAIN 1751..1967 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..24 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1968 AA; 216770 MW; 075E5C420D0C96A3 CRC64; MFGRKRALAS IGQQTSTDLR YHEPQSSWTD GDRIFTRELI RSGNGASKAV LTVRLAAEHP SRTSLDRLAH EYHLKDELDR EWAAKPLDFT TENGRIVLVL EDCGGVPLPQ LMGRHSHGMA DELTVFLRLA KGIAAAVGKA HGCGLIHRDI KPANILADEA EGRVRLTGFG VASHLSRERQ AAEPPEVIAG SLAYMAPEQT GRMNRSVDSR SDLYAVGITL YEMITGQLPF TASDPMEWVH CHVARRPVPP SDRVKELPGV ISAIVMKLLA KNAEERYQTA AGLEADLRRA LVQSEKNGRI AEFPLGTRDV PDRLVIPERP YGREREIAAL TSAFDRVVAG AGPTLVLVSG HAGVGKSMVV NELHRALVPP RGLFASGKFD QNQRHIPYAS VAQALQGLVR VLLGKSEAEL APWRAALTEE LGASGRLLVT LIPELESVIG RFPAVADLPP QDAKRRFQLN IRRLLRVFAT AEHPLTLFLD DLQWLDAATL DLLEDLCTQQ DMRHLLLIGA YRDNEVSPTH PLIRRLIAIR EAGGQVHEIV LTPLRLEDLT RMLADALHCG SNRVQPLARL VHKKSGGNPF FALQFLSALP DEGLLEFNGE QTHWDWDLDR IGAKGYTDNV VDLMLSKLRR LPDTTQAALN MLACLGNHAA VDTLALIRSE NHDAVHADFL AAARAGLVLL EEGSSYRFLH DRVQEAAYGL IPEDERAAAH LSIGRLLLMH TPPQALEENI FEIVGQLNCG GALIAPGEER ERLADLNLLA TRRARASAAY DSALAYAGTG AAYLPDDAWE RRYELAFGLE LHRAECEFLT GAPAEAQARL AELASRATSL ADLARVTRLR VDLFMSLGRS DQAIIFGLDY LHRVGISWSS HPTRSQVRQE YARLWRQLGG RPIEALLNSP PMADPVALAT MDVLTSLVTP ALFTNENLRC LVIGRMGNLS LKHGNSDTSP YAFTAVGTVL GPYFGNYEAG FRFGLLGLDL TEQPGMERLK ARVYLAFGNL AKSSSRHVRT GRALAQRVFE TAQQVGDLTY AVLSRNNLVT YLLAAGEPLS QVQRDAEAGL DFARQAGFGV AVGFISGQLQ LIRTLRGLTP IFGCFNDEGF DEQQFELKTD GKPGSCLYWI RKLQACVFAG DTLTALSAAA KAESLLWMTP AIFERAEYHF YTGLSLASAL QGSTTETALY GKAIRAHRRK LDTWAAHCPE NFASRAKLLG AEIARLGSRE LHAERLYEQA IQLAHEHALP HDEAIAYERA SAFYRARGFD QIARLYLQNA RRCYLSWGAD GKVRQLEEAY PQLRDGQLAP AATSTIEAPI EHLDLATVIK VSQAVSSEIV VEKLIDTVLR MAVEQAGAER GLLILSRGGE PRIAAEATIR GEAILIELRN EAITGVMPES VLNYVLRMRE IVSLDNVSAE NAFAADPYIR HRAARSILCL PLINHAKLIG ALYLENTLAG RVFAPGRIPV LKLIASQAAS TLEITGLYRD LAEREARIGR LVEANIIGIF IRDIGGRIIE ANEAFLQMVG YSRDELLAGQ LLDKELTPPE WRERDAKAEA ELRVTGSVRP FEKVYQRKDG GHVPVMIGEA SFEGAGSQAV AFVLDLSESK RAEERLRASE TRFRTFVDHA TDAFFLHTDD LTVIDVNRQA CESLGYSREE LIGMHPRDFD GAIDEKSLAT LVDRVDAGQP MTFETLHRRK DGTTFPVEVR VGKFRQEEQW FRLSLARDIT DRRQAEDAIQ LARAELAHVS RLTTMGELVA SIAHEVRQPL TGLVSSGNAC LRYLDADPRD IVSARRAIER MISDAFRASE VIDRIRAMAK KSPERRDRLN INDIVSETIA LVSTDLERSA VSLRTNLSDG LPPIVGDQVQ IQQVILNLIM NANDAMAATP KGARELVVST EKAAPNAVLV AVRDRGPILD LAKIGDIFEA FFSTKPKGMG MGLTISRSII EAHKGRLWAM PNAPHGAIFQ FTLPTEEK //