ID B1LXI7_METRJ Unreviewed; 862 AA.
AC B1LXI7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mrad2831_0742 {ECO:0000313|EMBL:ACB22753.1};
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:ACB22753.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB22753.1, 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; ACB22753.1; -; Genomic_DNA.
DR RefSeq; WP_012317746.1; NC_010505.1.
DR AlphaFoldDB; B1LXI7; -.
DR STRING; 426355.Mrad2831_0742; -.
DR KEGG; mrd:Mrad2831_0742; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_018130_0_0_5; -.
DR OrthoDB; 9797304at2; -.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACB22753.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ACB22753.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..862
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002766022"
FT TRANSMEM 42..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 602..819
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 812..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..849
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 94400 MW; 43B62D52F58950DE CRC64;
MGVGRATHVR IGVGALALTT ASAAFAELPE AAAAHPAREI HSVAALAIFG GLVAFAVILS
LLHLYERGRW TRRERELAAT LDVLRGAHDR AEMLLNAERQ IIVTWDQRSE PVVEGDISLA
IHGERPTSGY ARRVLAFGTW LVPADATAVE TAVETLRARG TGFALSLRSQ TGRSIEAHGQ
AVAGRALLRL RETSQERCEI ADLRAALDET RRGLSALSGL LDAIPQPVWR RNRDGGLSWV
NAAYVAAVEA ESREAALDAG LELFDRPARE TIAREEAARF AGLTRSVPRL SAIVAGNRRM
LDVFETGLET GRVGIAIDVS ELESVRADLQ RQMNANVRTL DQLPTAVAMF DVSQRLIFHN
AAYRQLWDLD QAFLDSRPSD GEILDHLRAE RKLEEHADFR GWKQGVLSAY RAAEANQTWW
YLPDGRTLRV VADPNPQGGL TYLFDDVSDR LNAESRYNAL RRLQAETLDT LAEPVAVFGA
DGRLSLANRA FFTVWRLDPE MVEERPHVDA VIAACRALAP AEEPWLDIRD AVVGLEARTA
RTCRLEVVDG TVLDCAAQPL PEGATLLTLI DVTASVNVER ALTEKNDALE KAAQLRDTFV
HHVSYELRSP LTNIIGFTQL LGDETVGALN ERQREYADHI MRSSAALLVI INDILDLASI
DAGSLELQRE EVDVQATVEA AVRGIEDRLA ESHITLALDV PEDIGSVHAD GKRVRQILFN
LLSNAVGFSD AGQRVEVQAR RTAQELLLSV RDHGRGMPPE IADSVFNRFE SHTLGTRHRG
VGLGLSIVRS FVELHGGRVL LETAPGSGTR VTCTFPTDHA GEARRAPPEP KAPLPPPPPR
KPILTLQPIR PEPPTSDRRT SP
//
