ID K9UK68_CHAP6 Unreviewed; 507 AA.
AC K9UK68;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cha6605_3846 {ECO:0000313|EMBL:AFY94816.1};
OS Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC Chamaesiphon.
OX NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY94816.1, ECO:0000313|Proteomes:UP000010366};
RN [1] {ECO:0000313|EMBL:AFY94816.1, ECO:0000313|Proteomes:UP000010366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
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 Chamaesiphon sp. PCC 6605.";
RL Submitted (MAY-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; CP003600; AFY94816.1; -; Genomic_DNA.
DR AlphaFoldDB; K9UK68; -.
DR STRING; 1173020.Cha6605_3846; -.
DR KEGG; cmp:Cha6605_3846; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR HOGENOM; CLU_570893_0_0_3; -.
DR Proteomes; UP000010366; Chromosome.
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; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00512; HisKA; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFY94816.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010366};
KW Transferase {ECO:0000313|EMBL:AFY94816.1}.
FT DOMAIN 19..187
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT DOMAIN 257..322
FT /note="Signal transduction histidine kinase
FT dimerisation/phosphoacceptor"
FT /evidence="ECO:0000259|SMART:SM00388"
FT REGION 210..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 55680 MW; 3E03CA4F4D638A21 CRC64;
MLNSEQDLDI NPDRQIARSR SLQSPPIVTE LSIEQSQVPI FAEATAQVAR LTDAPVAILT
AIAGSGDRIA SVYGLERLIL PTKPNLISEL AGLEYCHDRI FASQLSLSIV NFQQHPQLSQ
SSLCRRHELQ SYLGVPIITA ARDCLGTISI LDFKPRQFSD RDIELLQLVS RLVASEFERK
LLSQAQLERR LGNLHEQAKI GFDDPAVATE HNQSQVAKNA PQPAPASCLS DKKRASKLIP
TTAANCRLEP PQAQTQIQSK LLAHLAQELR TPLTSVLGMA SVLQQEIYGP LSSKQKDYLG
IIHHSGRQLV TIVDEISQLG GCDATTRQLT LKSVDLEMLC QLAIQSLESI ATKKQQQIKL
DLADNYSLAN SQPDESATPP IRVWLLDKDK VRQIVYYLCL SLIHVSGIDR HISIQFATMP
DGVEIQIATD DPNAILPNAD LSAQLTFDTS QSIEIDRHDL TDTKLGWDLR ISLGLSLSHT
LAASHGGKIQ SLSDGCGYCL ILPLIVN
//
