ID B1LWT7_METRJ Unreviewed; 925 AA.
AC B1LWT7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mrad2831_2229 {ECO:0000313|EMBL:ACB24224.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB24224.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB24224.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) 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};
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DR EMBL; CP001001; ACB24224.1; -; Genomic_DNA.
DR AlphaFoldDB; B1LWT7; -.
DR STRING; 426355.Mrad2831_2229; -.
DR KEGG; mrd:Mrad2831_2229; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_5; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000006589; Chromosome.
DR GO; GO:0016020; C: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 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; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 3.
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; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACB24224.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ACB24224.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 357..398
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 509..734
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 807..923
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 858
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 925 AA; 98154 MW; 010154023011C96C CRC64;
MADVTGPPAP AAGPQNSGPP VAQASALLGT GSIDRSEQPG RVGLLLVLAG LLVGAAIGLS
FVANEQAQSL IVWLLALLAM AGVFFLFALA IGALQLSGSA ARDDITKGIV DASPDGKLVV
EDGGRLIYAN EAYLRIASGD TFSNLVPVER ILVGSPEVSE AVYRLSQASR DARAHTEEVR
MSPPLGPTAG ERGFGWYRVS VRPLARPRRA ASLWTVADIT AERERQENVF QELQHAIDYL
DHAPAGFLSI DPAGAIVYMN ATLAAWLGYD LASVGPGGPH LTEIAPEADV LVRTAGLPGE
VRTDRFDLDL RRRNGHTLPV RLYHRVAFGK DGKPGSSRTF VINRSAGAET DEPQRAAEVR
LARFLNNSPI AIATLDSSGR IARANASFTR LFGTVPRQAD DGAPDGEGVP RVEPNVADSV
ADRTALEAGL ARAASGRTDP EPIEVQLNGP GGRSARVWLS PADGGDPGQQ TDEAERVILY
ALDTTAQRQL EQQVAQAQKM NAVGQLAGGI AHDFNNVLQA IIGYSDLLLA SHRPTDPAFQ
DIMQIKQNAN RAAGLVRQLL AFSRRQTLRP EVMNVGEALS ELTLLLKRLL GERVALELKH
GREVWPVKAD VNQFEQVIVN LAVNARDAMP EGGKLMIRTE NVSDPGAAAG AEGRGGAPAG
DHVLIEVRDT GQGIPPELME KIFEPFFTTK EIGKGTGLGL STVFGIVKQS GGTIDVQSKV
GEGTAFRIYL PRHVPVAEAE EVPVAAAEPA LPRAEPLAPT VLQPGADPTA KPATGSDGVA
PRGEAPPAKA DKPAPRKPAA DHTGQGTILL VEDEDPVRAV NSRALSARGY TVLEAASGLE
ALAIVREGAQ TIDLVVSDVV MPEMDGPTLL REVRKHQPDL KVIFVSGYAE DAFRKNLPEG
ETFNFLPKPF SLKQLVETVK KTMAD
//
