ID A0A126V4A8_9RHOB Unreviewed; 747 AA.
AC A0A126V4A8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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};
GN ORFNames=RC74_16820 {ECO:0000313|EMBL:AML52706.1};
OS Falsihalocynthiibacter arcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Falsihalocynthiibacter.
OX NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML52706.1, ECO:0000313|Proteomes:UP000070371};
RN [1] {ECO:0000313|EMBL:AML52706.1, ECO:0000313|Proteomes:UP000070371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML52706.1};
RA Lee Y.M., Baek K., Lee H.K., Shin S.C.;
RT "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t from
RT arctic marine sediment.";
RL Submitted (FEB-2016) 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 ---------------------------------------------------------------------------
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; CP014327; AML52706.1; -; Genomic_DNA.
DR RefSeq; WP_039003550.1; NZ_CP014327.1.
DR AlphaFoldDB; A0A126V4A8; -.
DR STRING; 1579316.RC74_16820; -.
DR KEGG; hat:RC74_16820; -.
DR Proteomes; UP000070371; Chromosome.
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.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AML52706.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000070371};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..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 513..739
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 747 AA; 82294 MW; 56C82AE906019CD4 CRC64;
MPSLVRSATF NRLIRLRRQK RFQNFATLGM VVLGPILAAA TFVILGPLEV ATSPNSLRLI
LLADMVYALV VAALVLQQVV RMVSARRAKS AGSKLHLRLT GVFALVTLLP TILVAVFAML
TVNVGIEGWF SDRVRQVVSS SLDAAQAYEA EHRRDLVSDA EQLGNDIDIE ALGNFRMSDG
DLREILTNAQ ANVQRGLREA FVVDGAGTIR ARGDRSYLFN YEQPKSSDFD KASKGETVVI
KDWENNEFRA LVALSGLTDR YLYLSREVDG DILSLLDETK QNVSLYEQLE KDRGKILFEF
GLLYLGFAVI LILAAIWLGL WFAERLARPV GRLTSAAQQV GAGNLNVRVY EEAGDDEIAL
LSQYFNQMTG QLREQRETLL QNTRQIEDRR RLFDSVLSSV TSGVVGLDAD GGVDFVNRSA
QGLLNLDDSG NQKLSLAVPE FGDFFARTQA NRAESAQEEV LVVRDGKQEN LLVRIAPRRG
SGGALEGYVV AFDDVTDLVS AQRMAAWGDV ARRIAHEIKN PLTPIQLSAE RLKRKYSSKL
SEEDAEGMAY MTDVIVRKTN DLRRIVDEFS KFARMPEPEL RSHDLTEIMR DAVHLQTGAL
DPVKLVAELP AEPIFADVDS TMIAQALTNL IKNAGEAVET HVENGVPDGF IPMVKINMEA
DGETLRIRIS DNGIGFPIDR SRLFEPYVTT RDKGTGLGLP IVKKIIEEHG GTLALLDAEI
FGNTTHAGAC VAVALPLGTP KKLKEVS
//
