ID C8RZ24_9RHOB Unreviewed; 758 AA.
AC C8RZ24;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Rsw2DRAFT_1052 {ECO:0000313|EMBL:EEW25981.1};
OS Rhodobacter sp. SW2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW25981.1, ECO:0000313|Proteomes:UP000010121};
RN [1] {ECO:0000313|EMBL:EEW25981.1, ECO:0000313|Proteomes:UP000010121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW2 {ECO:0000313|EMBL:EEW25981.1,
RC ECO:0000313|Proteomes:UP000010121};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Emerson D.;
RT "The draft genome of Rhodobacter sp. SW2.";
RL Submitted (AUG-2009) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EEW25981.1}.
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; ACYY01000005; EEW25981.1; -; Genomic_DNA.
DR AlphaFoldDB; C8RZ24; -.
DR STRING; 371731.Rsw2DRAFT_1052; -.
DR eggNOG; COG5000; Bacteria.
DR OrthoDB; 9776727at2; -.
DR Proteomes; UP000010121; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF00989; PAS; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEW25981.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 324..377
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 389..427
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 514..739
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 737..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 83016 MW; 9122EEA223F49860 CRC64;
MRSAVQNSTW NRLLRLRRQK RVQTAMTLGL VVLGPALAVA TFLALGPFNQ GANSPWLRLT
LLADLVYVLV VAALVLGRVM RIVADRRSQS AGSRLHLRLS GVFALLALTP TVLIAVFAVL
TLNVGVEGWF SDRVRQVVGN SLAAAEAYEG EHVRGLSEDA EAFAAYLNVA KQSTFFLEDA
QLRPVLTQGQ GQIQRGLRAA FLIDGGGTLR TRGEKSYLFD FTAPTPEEIA RAKAGETVII
QDWPNNEFRA LVHLDAYADR FLFISRKVDG SILSLLDETR ETVRLYHQLE SERGRLLFEF
GLLYLGFALI LILAAIWLGL WFAERLSRPV GRLAGAAQRV GGGDLDVQVL EEEGDDEIAM
LGRLFNQMTR QLKGQRDALV AGNRQTEDRR RLFDSVLSSV TAGVIGLDAR GRVDFVNPAA
ERLLAFTDGT PDRALALAVP EFAPLFQRLQ QSHGGAVQEE VRLTRGGRME SLLVRMSVRR
TDQGRLEGYV VAFDDVTDLV SAQRMAAWGD VARRIAHEIK NPLTPIQLSA ERIKRKFRPL
VGDQGEDLDQ YADVIIRQTN DLRRIVDEFS KFARLPEPDC HEHDLGAILR DAVLLQQAGQ
PGVSIKTDLP SEPVVLEVDA TMISQALTNL IKNAGEAIES LQEKGVPAGF APEVRVAFTA
DEQTAVIRIS DNGIGLPPDR ARLFEPYVTT RAKGTGLGLP IVKKIIEEHG GTLILTDAAV
FEGNSHAGAM AEIRLPRGPR ATKARPGKNA GLVGQGDT
//
