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Database: UniProt
Entry: A0A1J0ADN6_9CYAN
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Original site: A0A1J0ADN6_9CYAN 
ID   A0A1J0ADN6_9CYAN        Unreviewed;       595 AA.
AC   A0A1J0ADN6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=nblS {ECO:0000313|EMBL:APB34033.1};
GN   ORFNames=GlitD10_1708 {ECO:0000313|EMBL:APB34033.1};
OS   Gloeomargarita lithophora Alchichica-D10.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gloeomargaritales;
OC   Gloeomargaritaceae; Gloeomargarita.
OX   NCBI_TaxID=1188229 {ECO:0000313|EMBL:APB34033.1, ECO:0000313|Proteomes:UP000180235};
RN   [1] {ECO:0000313|EMBL:APB34033.1, ECO:0000313|Proteomes:UP000180235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D10 {ECO:0000313|EMBL:APB34033.1,
RC   ECO:0000313|Proteomes:UP000180235};
RA   Moreira D., Tavera R., Benzerara K., Skouri-Panet F., Couradeau E.,
RA   Gerard E., Loussert C., Novelo E., Zivanovic Y., Lopez-Garcia P.;
RT   "Description of Gloeomargarita lithophora gen. nov., sp. nov., a thylakoid-
RT   bearing basal-branching cyanobacterium with intracellular carbonates, and
RT   proposal for Gloeomargaritales ord. nov.";
RL   Submitted (OCT-2016) 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; CP017675; APB34033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J0ADN6; -.
DR   STRING; 1188229.GlitD10_1708; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000180235; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP 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; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:APB34033.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000180235};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:APB34033.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..595
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009608736"
FT   TRANSMEM        165..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          186..238
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          247..301
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          379..595
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   595 AA;  66257 MW;  CB86FB565169DC7B CRC64;
     MAAATLVVSL LMSLLTFWAV NSIQQDARMN DTRFGRDLGL LLAANVAPLV AQNNRTELAR
     LSEKFYNSTA SIRYLLYADT QGEIYFGIPF SAVEVQNSLT LRRRIQLPEL AAPDQPFVRQ
     HLTPDGLIAD VFVPLLQNEK YLGILALGIN PNPTVLSASL LTRNITLAVF ISIWILVILG
     GLFNAVTITR PIRELLVGVK NITSGDFRQR IDLPFGGELG ELIVSFNEMA ERLAHYEEQN
     IEELTTQKAK LDTLMSTIAD GAILLDCELK IVLINPIAEK IFGWSGQDVL GQEAFIALPK
     PVAETLAQPL VDLTQHGEAN GEPEEFCIHI QSPYKCTVKI LLTTVFDHLR NQLQGIAITV
     QDVTREMELN EAKSHFISNV SHELRTPLFN IKSFIETLYE YGHSLSEEQK RDFLETANKE
     TDRLTRLVND VLDISRLESG KPYPLTPTAL SAVVEQTLRA HRLTAKDKEI YLSAVMEPDL
     PDVIGHYDLL LQVLANLVGN ALKFTPAGGH VILWAYPWAG RVRVEVSDTG IGIPSEHQDA
     IFGRFFRVEN RVHTLEGTGL GLSIVQNILQ KHHTDIQLLS EVGIGSSFWF DLDQA
//
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