ID A0A1U9REI8_9GAMM Unreviewed; 635 AA.
AC A0A1U9REI8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B2G49_19400 {ECO:0000313|EMBL:AQU84563.1};
OS Halomonas sp. 'Soap Lake #7'.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1962264 {ECO:0000313|EMBL:AQU84563.1, ECO:0000313|Proteomes:UP000189672};
RN [1] {ECO:0000313|EMBL:AQU84563.1, ECO:0000313|Proteomes:UP000189672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soap Lake #7 {ECO:0000313|EMBL:AQU84563.1,
RC ECO:0000313|Proteomes:UP000189672};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AQU84563.1, ECO:0000313|Proteomes:UP000189672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soap Lake #7 {ECO:0000313|EMBL:AQU84563.1,
RC ECO:0000313|Proteomes:UP000189672};
RA Mormile M.R.;
RT "Halomonas from Soap Lake, Washington USA.";
RL Submitted (MAR-2017) 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}.
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DR EMBL; CP019915; AQU84563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9REI8; -.
DR STRING; 1962264.B2G49_19400; -.
DR KEGG; haso:B2G49_19400; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000189672; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
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; IPR033479; dCache_1.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR017055; Sig_transdc_His_kinase_DctB.
DR PANTHER; PTHR43065:SF46; C4-DICARBOXYLATE TRANSPORT SENSOR PROTEIN DCTB; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PIRSF; PIRSF036431; STHK_DctB; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AQU84563.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:AQU84563.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 303..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 405..618
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 369..396
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 635 AA; 71147 MW; AF550D718D736E0F CRC64;
MISQPLRWRL LWLIVIFLGL MLCMWQASLI AREQALSNLQ NDAENELRLS AANLNGYLLR
YDYLPRMLAT REGIQRYLAS PDSQDSMPLN MLLDRFRFTA GVSDIYLLDR HADTIAASNW
HRPNTFIGQN YAFRSYYTDA IQGGQGRFYG LGVQSLERGY YFSSPVWLDD TSPDAQPDGV
LVIKVLLDDV EASWAEQDAE LLVTDSDNII FMASHPELRM NALHPLSDDE RDALRATRRY
AMEPLSPSGI VLDTPYGPDS YLVSFSHGPL SGERYLSLTR PIPEFGWQMH ILKPLTPVIS
AQWIAALMAG GLYGIVALGG GIGWQRLRLR REREAFAERE RQTLARVRDE LEVSVELRTR
DLVASNQRLS GEIEERRRAE ASLRQTQDEL IQAAKLAVLG QLAAGINHEL NQPLAAIRAY
AENARRFIEL ARIEKADANL EQIVELTQRM ADISAQLRQF SRKSSERHEI ISVQACIEYA
LRLFHSRLKD GSVQVQQHWP EETLWVKADL VRLEQVLVNL IGNALQAMKE TLSPVLTLRV
EVVREHVVIS VADNGPGIAK PHLGQIFEPF FTTKAPGSGL GLGLSISSRI MDDLGGKLQA
TNQTAGGACF TVTLPYSSPP DSLATPLVKE NNNHA
//