ID A0A3L9Y158_9RHOB Unreviewed; 783 AA.
AC A0A3L9Y158;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D9R08_10555 {ECO:0000313|EMBL:RMA42182.1};
OS Rhodophyticola porphyridii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodophyticola.
OX NCBI_TaxID=1852017 {ECO:0000313|EMBL:RMA42182.1, ECO:0000313|Proteomes:UP000281343};
RN [1] {ECO:0000313|EMBL:RMA42182.1, ECO:0000313|Proteomes:UP000281343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA-7-27 {ECO:0000313|EMBL:RMA42182.1,
RC ECO:0000313|Proteomes:UP000281343};
RA Jung H.S., Jeon C.O.;
RL Submitted (OCT-2018) 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 -!- 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:RMA42182.1}.
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DR EMBL; RCNT01000005; RMA42182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L9Y158; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000281343; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000281343};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 394..617
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 666..782
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 641..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 717
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 783 AA; 84809 MW; 0350733CDCF549B6 CRC64;
MRVPLGAAPR QPWLLFGMAA ICAAAGWFVP SPLGALLLFA ASGSIAVLAL MLMARTHLGK
SGERRALIQA ISLIELDPAP CFCTDEQGLV LAQNISATDR FGDRAGQPMS RALSGLLANA
PAVVFRQETT LSRTRMARET VVTRKGHVRV TAYRVGKGTL WRLDESVEST NRSGDHIALP
MMVVSQNDTI LSMNDAMRDT LGRRARSLSQ VFRQLPLIPG QRRSLRTETG TIDVTPVEIR
AGDGRREIYL VPACVSGSIG DEGVAARAFE ALPVALVHIG GDGEVLAFNQ HAQTLLGLSP
GEGPFLSNLV EGLGRPIEDW IRDTLEERIP NRPEVVRAKR RDEDCFLQIT LGRIATSKGP
SLLAVMHDAT ELKTLEQQFV QSQKMQAIGE LAGGVAHDFN NLLTAITGHC DLLLLRHDQG
DPDYGDLVQI NQNANRAASL VGQLLAFSRK QTLQPELLDL RDTMGDLTHL LNRLVGEKVQ
LHLSHDPALL PIRADSRQLD QVMMNLVVNA RDAMPDGGAI HVETRMVRLR EALSRDEAVV
PPGQYVSITV RDEGSGIPAD KVRRIFEPFY TTKGVGEGTG LGLSMVYGII KQTGGYIFVD
SEIGKGTTFT IYCPAHDHPA AEESPVPSER PATAVPERIA QPPAPAEPEA PEAEQDTGPA
APGDGVVLLV EDEAPVRAFA SRALRLRGYT VLEAENAEEA LETLRDSALS VDVFVTDVVM
PGMDGPSWVR LALKDRPGVK VVFVSGYAED ALDKTSEEIP NSVFLPKPFS LSDLTATVQR
QLH
//
