ID H0TAK2_9BRAD Unreviewed; 1107 AA.
AC H0TAK2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BRAS3809_7510014 {ECO:0000313|EMBL:CCE03479.1};
OS Bradyrhizobium sp. STM 3809.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551936 {ECO:0000313|EMBL:CCE03479.1, ECO:0000313|Proteomes:UP000004098};
RN [1] {ECO:0000313|Proteomes:UP000004098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 3809 {ECO:0000313|Proteomes:UP000004098};
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 -!- 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:CCE03479.1}.
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DR EMBL; CAFJ01000725; CCE03479.1; -; Genomic_DNA.
DR AlphaFoldDB; H0TAK2; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000004098; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 2.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 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; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50885; HAMP; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCE03479.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 50..102
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 142..194
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 438..671
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 720..833
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 842..958
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 988..1105
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 362..428
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 769
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 891
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1038
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1107 AA; 120867 MW; 1A10C5EC2C5D1AF3 CRC64;
MVDQLNAFAG EVTRVAREVG TEGKLGGQAQ VPGVAGTWKD LTDTVNFMAA NLTEQVRGIV
KVVTAVANGD LKQNLTVKSK GEVAALAETI NNMTETLATF ADQVTSVARE VGVEGRLGGQ
ANVPGAAGTW KDLTGNVNLL AANLTSQVRA IAEVATAVTK GDLTRSIQVD ARGEVAELKD
NINTMITNLR LTTDLNTEQD WLKTNLAKFT NMLQGQRDLT TVGRLLLTEL TPLVNAHRGV
IYQVESEYMP QLRLLASYAN DGVYPHRQLV QFGEGLIGQC AIDKRQRLIA EIPADVIPVG
SALLRAVPKN LVVLPVLFEN QVKAVIELAS LSPFTTSQMT FLEQLTDSIG IVLNSIEATM
QTEGLLKQSQ QLAAELQAQQ RELQQTNEQL EQKAQQLAER NVEVERKNQE IEQARRALEE
KATELALTSK YKSEFLANMS HELRTPLNSI LILGQQLTEN PDGNLTMKQV EFARTIHGAG
TDLLNLISDI LDLSKIESGT VTVDAEEILT ANLLDTVGRP FRHEAENRLL SFNIDVDPNL
ARSIVTDSKR LQQVLKNLLS NAFKFTADGG VRLKVSAALG GWSADHPVLN TTPAVIAFEV
TDTGIGIPQD KQKLIFEAFQ QADAGTSRKY GGTGLGLAIS RELANLLGGE IHLRSAPGKG
STFTLYLPLK YSGPATTPRV SPPAPIPHVQ TPALQQSTAP ERVIEPLPDD RIDLAPGDTI
LLVVEDDPHY ARVLVDLARD KGFKVLVASR GAEALELAKQ YQPAAISLDV FLPDMLGWTV
LSQLKHNPLT RHIPVQIITL DEDRQHALAR GAFSFVSKPT TTEGVSAALS QIKEYAKPRR
KRLLIVEDND AERMSIRQLL EHDDIEILVA DTGAAALDAL RSAPCDCVVL DLRLPDMSGF
DVLDQLRSDE TLAGVPVVVF TGRELSAEED AELHTMARSI VVKGVESPER LLDETSLFLH
RVITELPAEK QRMLEKLNSS DEDLVGKTVL LVDDDARNIF ALSSVLERRG MKVLTAITGS
EAIDLVQRNP EIAIVLMDIM MPQMDGYQTI GVIRQSPTFA RLPIIALTAK AMKGDREKCL
EAGASDYLAK PVNTEQLLLA IRMWLHR
//
