ID H0TGY0_9BRAD Unreviewed; 857 AA.
AC H0TGY0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BRAS3843_1460026 {ECO:0000313|EMBL:CCE05718.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE05718.1, ECO:0000313|Proteomes:UP000002686};
RN [1] {ECO:0000313|Proteomes:UP000002686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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}.
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:CCE05718.1}.
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DR EMBL; CAFK01000053; CCE05718.1; -; Genomic_DNA.
DR RefSeq; WP_008968241.1; NZ_CAFK01000053.1.
DR AlphaFoldDB; H0TGY0; -.
DR OrthoDB; 9791542at2; -.
DR Proteomes; UP000002686; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd00088; HPT; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12915; PDC2_DGC_like; 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; 2.
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; IPR036641; HPT_dom_sf.
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 PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 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:CCE05718.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002686};
KW Transferase {ECO:0000313|EMBL:CCE05718.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..556
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 586..703
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 760..853
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 635
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 799
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 857 AA; 92773 MW; 27D523D14D6F3B0D CRC64;
MAASKRVLGV PAAIALALIG IIAGSNLFFL SNLRERALQE SEEELSRYSL TLAENADRSL
KSVDLVLSSV GDYLVRRGAV DATTFRVAAS DIETHHLLKE KIAGLPQLDA VTLIDAQGKL
LNFSRYWPIP DVNISDRDYF TTLKADTAPG TVISMPYQNR GDGTWNFYLA RRLNDAKGEF
MGLMLGALSV PYLENVFGST SLGLDANVAL LRDDGVMIAH FPPVNELGSP SSGFGQRTLA
AGGVLREPSR KTGEARLRAA KMLPSYPATV VVSVSQEHAL RSWRAMATLL TIMSLVSTVA
VLAAAVLITR WWRRHEHLIH AAEAANAAKS TFVAMMSHEI RTPMNAVLGL ATTLLETDLD
PEQRRSVVAI HNAGDSLLEI LNDILDFSKL ESGQLSLEDI GFSAEAMVHN ALSIIGPRAA
AKDLTIRSVI DPELPPALIG DAGRIRQILL NLVSNAVKFT AAGEVIVTTS CVARDGQKAT
IEWSVSDTGI GIAPEKIRTL FANFVQADAS INRRFGGSGL GLAICKRLTE QMGGEINVSS
TLGRGSTFSF RLTLPIAETA AAPEQNDDGI FAALQSRIAA FGRPLRVLVV DDNPTNRLVA
TKMLKEFDIQ TDTACDGAEA VTAANRFNYD LILMDVRMPE MDGFQATRTI RARGERRSEV
PIIAFTANAF MEDIRACREA GMNDFVVKPA RKKALVEAIL RVLPIPMSSA ARDTLKGSAA
PPLQPTETSG SLATLRLETE VAPEPALDHE AYAELQGEIG EEAAREIHSV FISETDARLK
LLRELSLNRE RIRIGREAHS LKSAAGTFGY RRLASLALAL EKSAPRLSKE DYAELLDSID
AAYAAARAQE LEETQPN
//
