ID A0A126RRS2_9SPHN Unreviewed; 607 AA.
AC A0A126RRS2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=K426_19150 {ECO:0000313|EMBL:AMK24759.1};
OS Sphingobium sp. TKS.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1315974 {ECO:0000313|EMBL:AMK24759.1, ECO:0000313|Proteomes:UP000060779};
RN [1] {ECO:0000313|Proteomes:UP000060779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKS {ECO:0000313|Proteomes:UP000060779};
RA Tabata M.;
RT "Whole genome sequence of gamma-HCH degrading bacterium Sphingobium sp.
RT TKS.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMK24759.1, ECO:0000313|Proteomes:UP000060779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKS {ECO:0000313|EMBL:AMK24759.1,
RC ECO:0000313|Proteomes:UP000060779};
RX PubMed=27056231;
RA Tabata M., Ohhata S., Kawasumi T., Nikawadori Y., Kishida K., Sato T.,
RA Ohtsubo Y., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane Degrader,
RT Sphingobium sp. Strain TKS, Isolated from a gamma-Hexachlorocyclohexane-
RT Degrading Microbial Community.";
RL Genome Announc. 4:0-0(2016).
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; CP005083; AMK24759.1; -; Genomic_DNA.
DR RefSeq; WP_021243106.1; NZ_CP005083.1.
DR AlphaFoldDB; A0A126RRS2; -.
DR STRING; 1315974.K426_19150; -.
DR KEGG; spht:K426_19150; -.
DR PATRIC; fig|1315974.3.peg.4022; -.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000060779; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.250.2580; -; 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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
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; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AMK24759.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000060779};
KW Transferase {ECO:0000313|EMBL:AMK24759.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..165
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 185..237
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 238..308
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 306..365
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 385..600
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 607 AA; 66301 MW; B52447183DE7A663 CRC64;
MTASLAGLAI AVIAVVTRWQ LGRQIDESVH YFVSLGVAGM VLVALRPDIV VLAGVTLVTL
TTLAIVDGWP TVAEQWVALF LFLAAMALLW RNHHRTLSRA RDLADGTRML AAELNLLIDG
AEDYAIYMLD AEGRVTIWNG GAERLKGWTE VEMAGQLTDR FYPADVVASG KPTSLLAEAQ
HRGKIEIDEW QIRKDGSEFL AHISITALKK PDGSLGGFAT VVHDITDQRA TLSSLRNSEA
HLRSILSTVP DAMIVIDEGG TMVSFSTAAE RLFGYTQEEV LGSNVSMLMP SPYRERHDGF
LERYLRTGER RIIGIGRVVF ALRKDGTTFP MELSVGEAAG ESQRLFTGFI RDLTDRQRTQ
ERLEQLQSEL IHVARVSAMG TMASTLAHEL NQPITAVANY LEAVRDLLDQ PDPDDLPDIR
EALTDAAGEA MRAGHIVRRL RDFVARGEVE KTVENLPNLI NEAAAFGLMG AGEKSIETRM
DIDHEAATVL VDKVQIQQVL VNLIRNAVEA MNARARPVLT IRTGPDQAGF VRVTVSDTGT
GMAPEVAAQL FKAFVSTKSD GMGLGLSICR TIVEANGGRI WMEPAEGGGT QFHFTLVRAD
REQSYGG
//
