ID A0A0Q5Z953_9BRAD Unreviewed; 1202 AA.
AC A0A0Q5Z953;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG57_33280 {ECO:0000313|EMBL:KQT14444.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT14444.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT14444.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT14444.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT14444.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT14444.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT14444.1}.
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DR EMBL; LMQJ01000028; KQT14444.1; -; Genomic_DNA.
DR RefSeq; WP_057197640.1; NZ_LMQJ01000028.1.
DR AlphaFoldDB; A0A0Q5Z953; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000051536; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
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; 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQT14444.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
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 361..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 380..431
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 453..523
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 526..578
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 579..649
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 701..772
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 779..829
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 842..1064
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1084..1200
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 416..443
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1134
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1202 AA; 131210 MW; 3205DC07F0B8D7B8 CRC64;
MSAPAADDKN APSAPGQTWR GGTAIAANVP MRLATTLATR LAVAMILLVA ITVAAVGWLG
YRNTTQAVIP RVLERVEAQA RLLASNLQSY ADGVRGDLIG YRAAAAIKGL IRAHAAGGID
PSDGVSEQTW RERIATRLVA EIEAKPIYGQ FRIIGIDNGQ RELVRVDRSG PNGAARIAPD
DELERKGDRA YFQETIRLRP GEIYVSSVDL ATRRGGTTTP HVPTLRVAMP LFTDDDRPFG
IIVANIDMRP ALDHVRSTVR SGGEIYVVNS RGGYLLHPDR TRELGASHDR PTDWRKDFPY
FAALAGTLDV STRLLTDESG RPSGAAIAPA LLAGKEWVAI IETIPAPVFG LVPAAIQRTS
LLVGVLAVLA AAALAVLLAR SLTRPIGRLT AAVQAIGSGR PADIPVDAGG ETGVLARAFA
QMVEETRAKA AALEREIEEH RRTEAARSHH AARESLFSAA VESSDDAIVM QTLEAVITGW
NPAAERLYGY TAEEAIGKPT SIIVPPDRRE QGKDYLRRIA RGEPIERFET VRLRKDGTPV
EISLGLSPIK GPSGEIIGAS GSARSLTEAR RAERALQHQL EERRQIFETS QDLIMIMDAR
GHIAQISPSS EAILGYRPEE MTGRSGADFI HPDHLETSRD EMRALRRGER PKLADTRCFH
KNGHEVWLSW LGSWSEPAHR FFFVGRDMTE ARLAQESLRE SERLARNIVE TSLDAFVQTD
ETSSILNWNS RAEQLFGWHR DEVLGKRTID LIVAESERER VRSGLKRFLE NADGGTLNRR
HELMCRRRDG KEFKAELSVT ALKRREGLLF NVFYRDLTDK IAAEERIRHV EKMEAIGQLT
GGVAHDFNNI LTVITGTIEI LAEAVEKEPQ LAAITKMIDE AAARGADLTQ HLLAFARKQP
LQPREIDINS LIVDTAKLLR PTLGEQVQIE SVFEDENCVA IVDPNQLTTA ILNLALNARD
AMPGGGKLIL ETGVAYLDEV YASANDMPPG HYVLIAVSDT GTGIPANMLT RVFDPFFTSK
GPGKGTGLGL SMVYGFIKQS AGHIKIYSEE GHGTTIKMYL PPGKTPTAAG EGVAPATIEG
GHETILVVED DQLVRDYVLA QLHSLGYVTL QAANAAEALA IVAAGKPFDL LFTDVIMPGK
MNGRQLADEV MKTRPDLKVV YTSGYTENAI IHHGRLDTGV LLLAKPYRKS DLARIIRKAL
QS
//
