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Database: UniProt
Entry: A0A2K8TAG4_9NOSO
LinkDB: A0A2K8TAG4_9NOSO
Original site: A0A2K8TAG4_9NOSO 
ID   A0A2K8TAG4_9NOSO        Unreviewed;       601 AA.
AC   A0A2K8TAG4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=COO91_10889 {ECO:0000313|EMBL:AUB44651.1};
OS   Nostoc flagelliforme CCNUN1.
OG   Plasmid pnfsy08 {ECO:0000313|Proteomes:UP000232003}.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB44651.1, ECO:0000313|Proteomes:UP000232003};
RN   [1] {ECO:0000313|EMBL:AUB44651.1, ECO:0000313|Proteomes:UP000232003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB44651.1,
RC   ECO:0000313|Proteomes:UP000232003};
RC   PLASMID=pnfsy08 {ECO:0000313|Proteomes:UP000232003};
RA   Shang J.;
RT   "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT   its photosynthetic adaptation to extreme terrestrial habitat.";
RL   Submitted (NOV-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};
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DR   EMBL; CP024793; AUB44651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8TAG4; -.
DR   KEGG; nfl:COO91_10889; -.
DR   Proteomes; UP000232003; Plasmid pnfsy08.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; 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   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AUB44651.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:AUB44651.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232003};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AUB44651.1};
KW   Transferase {ECO:0000313|EMBL:AUB44651.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          340..597
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          294..321
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   601 AA;  67674 MW;  EE990595DCB1A0A1 CRC64;
     MSRRNVAFFS TIHALALLAP WYFSWSALGV AGALYWLFGS IGICLGYHRL LTHRSFQVPK
     ALEYAFTGFR YRYQKWEATG KVQQLDEQYS QLFTNTVAKV NGRGTITKQI QDISEAKTQT
     LDISTAIKAS QALSSEMELN RLLEKIMTIA IENAGAQMGY LLVKRENQWV IEAEGSIDRD
     RVTVRSSSLF QVKHKLPVLL INYVERTKEN LVLDDASHTE RFMSDNYIVA NQPKSILCLP
     FSDQGKLTGV LYLENNLTTG VFTAERLEVL NLLTSQVSIS IENARLYTNL HIYSQELEIS
     ETEAREKAKQ LEHTLDELKL TQSQMVQSEK MSSLGQLVAG VAHEINNPVS FIYGNLTYVN
     NYVKDLMSIV QLYQQQNQNL PPKVQNEIDA VDLDFLMEDL PKLLASMRVG TDRIRQIVLS
     LRNFSRLDEA EVKGVDIHEG IDSTLMILQN RLKPEPNSPG IQVIQEYGNL PPVECYPGQL
     NQVFMNLIAN SIDSLEEFNK YRTYADIARQ PSIITIRTTV EGDFAVIRIA DNGSGISENV
     LPQLFTPFFT TKPVGKGTGL GLSISYQIVT KKHRGQLECV PVLGQGAEFM ISIPLARQGE
     Q
//
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