ID S5SSA5_RHIET Unreviewed; 858 AA.
AC S5SSA5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=kdpD {ECO:0000313|EMBL:AGS24887.1};
GN ORFNames=REMIM1_PD00276 {ECO:0000313|EMBL:AGS24887.1};
OS Rhizobium etli bv. mimosae str. Mim1.
OG Plasmid pRetMIM1d {ECO:0000313|EMBL:AGS24887.1,
OG ECO:0000313|Proteomes:UP000015261}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=1328306 {ECO:0000313|EMBL:AGS24887.1, ECO:0000313|Proteomes:UP000015261};
RN [1] {ECO:0000313|EMBL:AGS24887.1, ECO:0000313|Proteomes:UP000015261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mim1 {ECO:0000313|EMBL:AGS24887.1,
RC ECO:0000313|Proteomes:UP000015261};
RC PLASMID=Plasmid pRetMIM1d {ECO:0000313|Proteomes:UP000015261};
RA Rogel M.A., Bustos P., Santamaria R.I., Gonzalez V., Romero D.,
RA Cevallos M.A., Lozano L., Ormeno-Orrillo E., Martinez-Romero E.;
RT "Genomic basis of Rhizobium etli symbiovar mimosae and its prevalence among
RT Phaseolus vulgaris nodule bacteria.";
RL Submitted (MAY-2013) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP005954; AGS24887.1; -; Genomic_DNA.
DR AlphaFoldDB; S5SSA5; -.
DR KEGG; rel:REMIM1_PD00276; -.
DR PATRIC; fig|1328306.3.peg.5278; -.
DR HOGENOM; CLU_000445_113_1_5; -.
DR Proteomes; UP000015261; Plasmid pRetMIM1d.
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 CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGS24887.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:AGS24887.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGS24887.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 632..849
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 858 AA; 93657 MW; 324EE44512F5F3D9 CRC64;
MLISGRAKIA DGHDVVIGVV ETHGRKETEA LVAGFEIIPR VEIDYKGRLL EEMDLDGILA
RRPDLVLVDE LAHTNAEGSR HPKRYLDVKE LLDRGIDVYT TLNIQHVESL NDVVSQITRI
RVRETVPDSI IDLADDVEII DLTPDDLIKR LHDGKVYMPK TAERALTNYF TPGNLTALRE
LALRKTAQRV DDQLLTHMQA HAISGPWAAG ERVLVSIDHH PRSASLVRYA ARMASRLRAP
WAAVYIETNR SINLSEAERD TIASTLRLAE QLGGEAITIP GREVAEELVR HASANNVTHI
VIGAPKKPTW RDWWGRSVTD ELIRKTGEIS VHVISGTEKD GTTARGIKAA AVAPQLDIRA
YLLATVYVAI ALGVSIVLDQ VLDVRNLALV FLMAVLTSAV LHGLRPALYS CILGALSFNF
FFLPPRYTLT ISDPESVLAF FFFLGVAIIA SNLTATVQRQ AAAARQRART TEDLYLFSKK
LAGTGTLDDV LWATAFQLAS MLKVRVVLLL PEEGSIAVKA GYPPDDTLDD ADIAAAGWAW
EHNHAAGRGA DTLPGAKRLY VPLRTGRTAV GVIGLDSDRR DGPLLTPEQQ RLLDALADQA
ALAIERVQLV ADVDRARLAA EADRLRSALL TSISHDLKTP LAAILGAAGT LRDYFASMPE
EDRSDLLSTV VDESERLNRF IANLLDMTKI ESGAMEPNSA LHYAGDIVGT ALARAAKILE
HHKTEMSIPA ELPMVRVDPV LFEQVIFNLL DNAAKYAPEG SVIQIEGWAD ADNVVVQISD
EGPGIPPADL ARVFDTFYRV RKGDQVRAGT GLGLSICRGF IEAMGGTITA GNRRGRPGAV
FTIRLPKPND IPKPDELK
//