ID K9RG58_9CYAN Unreviewed; 814 AA.
AC K9RG58;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Riv7116_3617 {ECO:0000313|EMBL:AFY56067.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY56067.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY56067.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY56067.1,
RC ECO:0000313|Proteomes:UP000010380};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-2012) 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};
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DR EMBL; CP003549; AFY56067.1; -; Genomic_DNA.
DR RefSeq; WP_015119633.1; NC_019678.1.
DR AlphaFoldDB; K9RG58; -.
DR STRING; 373994.Riv7116_3617; -.
DR KEGG; riv:Riv7116_3617; -.
DR PATRIC; fig|373994.3.peg.3849; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_346776_0_0_3; -.
DR OrthoDB; 434700at2; -.
DR Proteomes; UP000010380; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 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; SSF55781; GAF 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010380};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..136
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 532..795
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 814 AA; 90976 MW; 1339B1D3B937B1F7 CRC64;
MSYINHLRQT NSGQDMVHSQ FVKIARILVS LIVVAIFCGT GWLFTRDKEI LVSDSAFVIL
AEALIAIAVL VILVGRATKI IEAACTQRDK AVDALRENEA KFKSLVDASL VGIAEVNIDG
SINVANDEFL RITGYNFTCL QAGKLNWFDI APSELKDIDN NDCYQFQSVE NCKTYIKYLI
CADGRQIKVK LSRNHLETQG KPHKYIFYVS ECNHTEENSI FGQLWLKSLF DIMPVPLLLV
EPGTAKVTFA NQAANEMAGG QFPLAQSRED YSKLYRFTDT EGKLIPSELS PTIRVALGEK
LEGLEINWHE RDKVYPVKVF ADTLPPMPGY PSTCIALFED IGKLKQLEES LDLENERLKL
VFETTKDLTA SEQPEELIEE LYHEIAEQLD LDCYLYYLVD KNCQGIKLTS YSGITFSEAK
DFQQYKFGEG VSGTAAQKRS PINIENAPQS EDLDTQSIRN LGILAYYSCP LIVQEKLLGT
ISFASRTRSA FIDDEVILMQ AVCNQIAIAI ERANLLNSLQ KANRIKDEFL AILSHELRSP
LNSILGWAQY LQVRKLDEIT TSRALESIER NSRELNNVIE ELFDISRTIQ GKMQLTIQDC
NLASIIVTAI ENLRSASLAK KLEVKLSIHK SLDMNEHIEN AEFADTFDSL KHIASLNTIP
VPHEAILKNS DFLVAGDSQR LRQVMWNLLS NAIKFTSCGG CVEVHLLEEK TNDDELSYAV
IQVSDTGMGI NSEFIPYVFD RFCQGDSSST RAHNGLGLGL SIVRHIVELH GGSVCVESPG
VGEGSTFTVK LPLVKSTESQ SIKKKCQEKC VVIN
//
