ID K2C8K2_9BACT Unreviewed; 360 AA.
AC K2C8K2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=ACD_39C01360G0001 {ECO:0000313|EMBL:EKD82321.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD82321.1};
RN [1] {ECO:0000313|EMBL:EKD82321.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKD82321.1}.
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; AMFJ01015782; EKD82321.1; -; Genomic_DNA.
DR AlphaFoldDB; K2C8K2; -.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 1..217
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 230..348
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 281
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKD82321.1"
SQ SEQUENCE 360 AA; 39881 MW; 9F3A0A90A1E20DAC CRC64;
IPAEPLFRSL TAFIGIPALL KKRSDLPADV MESIRMLEKS GVKMLDMINK SMDLYKMEAG
TYKTCPVPVE LVRIVEQIGF ELSNYLSAKS IRLQICINDN EVSAGAKFYV RGEETLCYAM
LANFLKNALE ACPANETVKI SFFDEPRVRV TVNNPGVIPL EIRDKFLHKF ASHGKIGGTG
LGGYSARLMA QAMGGSVSFT SDEASGTTIV IDFAVDSRLA SAECNIGDLR ALVIDDNEML
LFTIREILRS IGLYRIETMA DTDSARAYLR SGQAVQLIIL DWNFSAGSCR ELFRRIRADE
DFKKVPLLVI SSEPVDEEVR VAIDEGSVEL LSKPFSPDLL LKKVEGFMAR MLQLCVKVVN
//
