ID Q124F5_POLSJ Unreviewed; 521 AA.
AC Q124F5;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Bpro_4195 {ECO:0000313|EMBL:ABE46087.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46087.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE46087.1; -; Genomic_DNA.
DR RefSeq; WP_011485076.1; NC_007948.1.
DR AlphaFoldDB; Q124F5; -.
DR STRING; 296591.Bpro_4195; -.
DR KEGG; pol:Bpro_4195; -.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_114_71_4; -.
DR OrthoDB; 8552871at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 2.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABE46087.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW Transferase {ECO:0000313|EMBL:ABE46087.1}.
FT DOMAIN 147..191
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 302..518
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 521 AA; 56360 MW; F9E8EE07BE80407B CRC64;
MSRFLNLFGV KLADKMPGLG VQNGSRSSAP AELGWGPLEQ SGDGMVLLDE RGRITEANPR
ALELLHCAQP ALAGLDFWEA VPEDITEQHQ SATGQALTFA ARHAFVAHDK FEDKWVRYAF
TRQPPGYVVS LRDVSSTQRL LDVLEDSERY NQLIFEANPN PMWIFDDSST RILAVNQAAV
EFYGIARKKF LTLGMDALFP EGEGAGWLSS LASGKGVGEG LLALRLCKQQ KADGQQVLVE
LACGPVSWNG QQAVFVSLAD VSQRHLADGA LRRANAELEQ ELAGCQSELE KTRRDVAAFT
RAVSHDLQGP LHAVNGFAKV LAKNYSTALD ASGLHYVSRI QASTRQMAKL VDDLRTLVQL
PELSGNPEKF DLVPICRALV DDLRKRAPDR SVAIEMDASL LLVGDKGLLT TALACLLENA
WKFTSKKAEA WIKVGLMPGA TPGELVLLVS DNGAGFDTAY SSKLFTPFQR LHSSAEFPGN
GLGLAIVKRV AARHGGNVWA ETTGQAGASF YLALPHAAQA A
//
