ID Q2K7J6_RHIEC Unreviewed; 440 AA.
AC Q2K7J6;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase MprB {ECO:0000256|ARBA:ARBA00040454};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Mycobacterial persistence regulator B {ECO:0000256|ARBA:ARBA00041776};
GN OrderedLocusNames=RHE_CH02412 {ECO:0000313|EMBL:ABC91190.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC91190.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC91190.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; CP000133; ABC91190.1; -; Genomic_DNA.
DR RefSeq; WP_011425669.1; NC_007761.1.
DR AlphaFoldDB; Q2K7J6; -.
DR KEGG; ret:RHE_CH02412; -.
DR eggNOG; COG0642; Bacteria.
DR HOGENOM; CLU_000445_89_27_5; -.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000001936; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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 PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABC91190.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 182..234
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 242..440
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 440 AA; 47776 MW; D1EC7E598E8FDADF CRC64;
MSASMSILPG LMWPRTLRSQ IFLILLIGLA FAYGLSFSVL YMERYMSAKA VMLGTLENDV
ATSIAVLDRL PASERGDLLD WLSRGNYRFE LGPGLLGVPD SSSKAREIAG KIEAAAGHRF
PIRVERIPGE VSRLQAHLTL SDGTPLTIDV TPRGVMPIAA WLPYVFAIQM ALLVLCTWFA
VRQAIRPLGE LAAAADALDP DKDGQALSEV GPSEVAHAAR AFNAMRERIA HYLEERVQIL
AAISHDLQTP ITRMRLRADM AEDSPERDKL VHDLAEIQRL VQDGIAYARS AHGSGEKNAR
IDLASFIDSI AYDYQDTGKA VTVVGLVEGA AFTRPHALRR ILSNFIDNAL KFAGAAEISV
ERGADNSVVM SVMDRGPGIP DDMLEAAMQP FFRLEQSRNR ETGGTGLGLA IAQQLTAKIG
GSLRLYNRSG GGLVAEVTIR
//
