ID A0A433URL8_ANAVA Unreviewed; 444 AA.
AC A0A433URL8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DSM107003_25910 {ECO:0000313|EMBL:RUS96494.1};
OS Trichormus variabilis SAG 1403-4b.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=447716 {ECO:0000313|EMBL:RUS96494.1, ECO:0000313|Proteomes:UP000276103};
RN [1] {ECO:0000313|EMBL:RUS96494.1, ECO:0000313|Proteomes:UP000276103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 1403-4b {ECO:0000313|EMBL:RUS96494.1,
RC ECO:0000313|Proteomes:UP000276103};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
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:RUS96494.1}.
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DR EMBL; RSCM01000007; RUS96494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433URL8; -.
DR OrthoDB; 568844at2; -.
DR Proteomes; UP000276103; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000276103}.
FT DOMAIN 6..122
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 180..399
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 116..170
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 444 AA; 49680 MW; 3F9FD8B88B0F279D CRC64;
MEETLKILVV NNDEADRMAV RLALAKAGIC MELHEVSEIN KALAALKSTN FDCVFLDNSL
PDQDGLNSIH KLRSSEIKVP LVILSAQGNE QIAVELMKAG ATDYLPKSKL SPETLAQTLR
NAIRLYRAEM EAALANQKLK ESYEQLLHKN QELEKQRQQI QLQNLKLLEA SRLKSQFLAT
ISHELRTPMN AIIGFSQILL RPKFAQLTNQ QADLVERILN NGKHLLMLLN EVLDFSKLES
GKLDLKPEIF DLSKIVNKTV EEIRSLAEAK KLSLVVKTDL QNTLVFNDPV RVHQIVINLL
SNAVKFTENG GIWVEVKETP NNRVTISIRD TGIGISPGDF EHIFEAFRQV DQGISRKYPG
TGLGLAIIDS LVQMMGGEIF LESQLEVGSI FIIELPRQVI LAPSLADSSS LNFGSDSLYY
SHNNHPQFPS KFSKYSLGYP NLKP
//
