ID A5EKX9_BRASB Unreviewed; 867 AA.
AC A5EKX9;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BBta_4799 {ECO:0000313|EMBL:ABQ36823.1};
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ36823.1, ECO:0000313|Proteomes:UP000000246};
RN [1] {ECO:0000313|EMBL:ABQ36823.1, ECO:0000313|Proteomes:UP000000246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000494; ABQ36823.1; -; Genomic_DNA.
DR RefSeq; WP_012044807.1; NC_009485.1.
DR AlphaFoldDB; A5EKX9; -.
DR STRING; 288000.BBta_4799; -.
DR KEGG; bbt:BBta_4799; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_21_5; -.
DR OrthoDB; 8169077at2; -.
DR Proteomes; UP000000246; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12915; PDC2_DGC_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; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
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; 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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 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; SM00091; PAS; 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; 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; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 430..482
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 495..719
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 741..856
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 791
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 867 AA; 94212 MW; 9D2230B462F90706 CRC64;
MLDQTKAQAG DQPASRHKGF AGALTRAEAR LGLNRRWTPR IIILSGLVLA VLCDAFVAHM
LSVNYRETYR TIKAANGDLA RALEEYMLRN IQGVDVLLSG TINNLAKNPA LLTAGNPALI
DELKQRVAPY PIANAIVVLD ADGKLLGDSL GNGGPGREQN FADRTYYKAQ RDDPGRGLFI
DVPVFSRVRN SLVLVVSRAF LTPEGRFGGI VFVPIDYENL RQFFLSLNVG QRGTVTLYRD
DGTILLRTPN ADEFAGRDVR SNRLFTYYLP QAQSGSFEGS GMTDGTSRSI SYRRVAGMPL
VVTIARDPVE FLAGWKNNAL YYSVIAAGLN LLIAGFGFGL ARQWRLRATS EQALRDNLEQ
HQLVTENVPA LIVHVLEDGR IRYANRVARD WYAAPSTDTI CGRKIEDFID PSHLDEARAK
IEAALAGRTT GGEEETTFPD GRERWCETIR VPDCRQDGTV RGYFVLSVDI TERKRIEDEL
RQAQKMEAIG QLAGGIAHDS NNMLAATLGN LDLLLDALPQ AEVSARSLAE RAAEAAERVA
DLNRRLLAFA RKQTLRPQVT DVNQLVCAMT TILQRTLGET IEIEVAQDPM LWQCLIDPTQ
LQNALLNLAL NARDAMAGQG RLTITTANAV LDQPLDDGDE RIGPGEYVTI AVADRGAGMP
PEIARRAFEP FFTTKEFGKG SGLGLSMVYG FARQSGGTAV IASQVGQGTQ VTLYLPSAGP
GASGEARAGT TRLPRPDRAE RILVVEDNPL VGAMASTMLS SMGYSPVVVV NAAAAIAELE
RPEPVALLLT DIVLPDGVTG IDLARQVRHR WPELPIVFMS GFADPSLVPE DFRATTKLLA
KPFRLGQLSE AIVSSLAGRP AAGRTAT
//
