ID A0A2T1E8L6_9CYAN Unreviewed; 1314 AA.
AC A0A2T1E8L6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C7B82_12285 {ECO:0000313|EMBL:PSB29086.1};
OS Stenomitos frigidus ULC18.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Stenomitos.
OX NCBI_TaxID=2107698 {ECO:0000313|EMBL:PSB29086.1, 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:PSB29086.1, ECO:0000313|Proteomes:UP000239576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC18 {ECO:0000313|EMBL:PSB29086.1,
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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:PSB29086.1}.
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DR EMBL; PVWK01000067; PSB29086.1; -; Genomic_DNA.
DR OrthoDB; 436952at2; -.
DR Proteomes; UP000239576; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR Gene3D; 1.10.1760.20; -; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
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; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000239576};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 570..643
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 644..696
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 716..852
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1067..1301
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 532..580
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1314 AA; 148007 MW; F82D7A77D3EA91D7 CRC64;
MGLAAVLQAK WLYKRNLLGL LLLVIAGFLG NYFRWTLFFD IDFLFGSIAV WLVVCLYGVR
WGTLAGFIAG SCTYVIWHHP YTTLTFTLEA LFVGWLFHRR QQQNIVLLDA AFWLLIGMPL
VWFFYAVVLH VDSAQVLIIL LKQPVNGIFN ALIASLLLTH LPIHRWVSRP PAIATLSLQQ
TLFNLLVAFV MVPTLILIVL ASHQVVNDIK TTARADLDDA TRYLTVEVRA WYERRLAVVN
ELAKLAVDVP EGDSVQGDRV RQKGEFAQRV FPDFRQIHVL DRTGRRILTA GDGATQAQGG
SDDTFYFKQL QRSPGALLSL VQPQPGSTAS PTAMLGVSIV RDGQSAGAVL SELDLSFITS
LLQANVGDRG LNITLVDQQN TVAASTRTEW IGNQSFDWRK QGKTEAIGEQ TYHWLPVSSP
LVMVQWNKSL FVKEVTISNK IPWRLIVQMT ATPHVQHIEM VHTRSMAILL VISGFAPLAA
IFVSRQLVKP VSQLATVTTN LPEKLLAQAS IQWPQSQVTE FALLVHNFRS MAASLQQKFG
EIQQANASLE QRVQERTEAL QQSNAALRES EARFRQMAEN IREVFWMGSV GKDSLTYISP
AYEAIWGRTC ASLYEDPRSF IDAIHPEDRA QVVAAFAKQR QGDYSEEYRI IQPNGSIRWI
WDQAVPIRDE AGAVHRIVGV AQDITERKQA EVIVRQQTER ERLLGAITLH MRQSLELDDI
LNTTVAEVRQ FLHTDRVVVY QFQPDWSGIV IVESVAEGWQ SLLGRQITHT YFAETQGEDY
KQGRILATND IYAAGLADCH LELLAQLQVR AELVVPILQG ETLWGLLVAQ HCCSPRTWQP
SEIDFLKQIA IQAAIAIQQA ELYQQEQRLN TILEQQVEER TAQLQQSLRY EAMIKRMTDK
VRDSLDEAQI LQTAVEELVH GLELYGCDTA LFNLEQGSMT LSHACTHEML APHPEVVLAT
NFSDIYPQLL VGQSLQFCEL VPPFMDAAWQ PRTIFACPII DDQGVLGKLR LFRDCEAIFS
ESEIRLALQV ANQCAIAVRQ ARLYQAAQVE VKALEELNRL KDDFLSTVSH ELRTPVSNMK
LAIHMLKTMP TEERRERYLE ILQTECTREA DLINDLLDLQ RVASGTRVLE LENIDLQAWL
EELLQPFQER AQTRQQRLQV NLSPRLTTWM SDRACLSRIV AELLNNACKY TPPNETITLS
IQPIDQSADS ETAQAQERII SLVATQLQLS VCNSGIEIPS GERDRIFAKF YRIPGTDRWQ
QGGTGLGLAL VQKLTEHIGG TIKLESDANW TCFIVELKAQ TPMTAMATST AAKP
//
