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Entry: A0A2T1E948_9CYAN
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ID   A0A2T1E948_9CYAN        Unreviewed;       609 AA.
AC   A0A2T1E948;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C7B82_11785 {ECO:0000313|EMBL:PSB29266.1};
OS   Stenomitos frigidus ULC18.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Stenomitos.
OX   NCBI_TaxID=2107698 {ECO:0000313|EMBL:PSB29266.1, ECO:0000313|Proteomes:UP000239576};
RN   [1] {ECO:0000313|Proteomes:UP000239576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULC18 {ECO:0000313|Proteomes:UP000239576};
RA   Moore K., Momper L.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB29266.1, ECO:0000313|Proteomes:UP000239576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULC18 {ECO:0000313|EMBL:PSB29266.1,
RC   ECO:0000313|Proteomes:UP000239576};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) 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};
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:PSB29266.1}.
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DR   EMBL; PVWK01000063; PSB29266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T1E948; -.
DR   OrthoDB; 445851at2; -.
DR   Proteomes; UP000239576; 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   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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13492; GAF_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:PSB29266.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239576};
KW   Transferase {ECO:0000313|EMBL:PSB29266.1}.
FT   DOMAIN          371..602
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          334..371
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   609 AA;  67636 MW;  903A8B9AB63EB2C6 CRC64;
     MTSPIDFQRS LSEGLAITSA KDQLPEFTDE LVFIQDTAGL YLAFHWQCAA HYNLLPENVV
     GSRLGEIFSP VELAPYRERL QRVLSRSAAE EFRSYFRCGE ETLLFDLVMS PVLIPHRSPT
     AVVVAGRLIL VPSDTAEAPQ LAEQSALDTV SLNSYAVLSS SSDRYQKLLT QIASNIRRTL
     DLPTIWQQTV QGLGKALGAS RCLVCPYEHR THEQRTSKVK VVAEYYQDTF PPMLGLEFWV
     ADHAVLAGAI ASLQPITVRG ESAFQGINAE CKQQSTLVVA TCYLDQPNGL IVLQQCDRDR
     EWTAAELELM QEMADQVGTA IAHATLFTAS NTLTADLQRA NASLIQKHRE LEEARRQAEE
     ASRLKSEFLA NTSHELRTPL NGMIGFLKLI LDGMADDPAE QNEFINEAYE SALHLLEIIT
     DVLDIAKIEA GTLQIELKSV DLNELLHDVQ RFAHSQMHLK KLSFEIQKPP TDDEIILFGD
     YLRLKQVMFN LVGNAIKFTH EGGVTISIEV IKKKIKFQNQ DLPGMVKVRV ADTGIGVSLD
     KQDRLFQSFS QIDGSRTRQY GGTGLGLAIS QKLVEAMGGD VHFYSMGEGL GSTVTFTALL
     YQEPVMITS
//
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