ID A0A2T1G5S3_9CYAN Unreviewed; 1116 AA.
AC A0A2T1G5S3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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 ORFNames=C7B67_06675 {ECO:0000313|EMBL:PSB52530.1};
OS filamentous cyanobacterium Phorm 6.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107706 {ECO:0000313|EMBL:PSB52530.1, ECO:0000313|Proteomes:UP000239157};
RN [1] {ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|Proteomes:UP000239157};
RA Moore K., Momper L.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB52530.1, ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|EMBL:PSB52530.1,
RC ECO:0000313|Proteomes:UP000239157};
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:PSB52530.1}.
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DR EMBL; PVWI01000037; PSB52530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1G5S3; -.
DR OrthoDB; 437650at2; -.
DR Proteomes; UP000239157; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
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 Gene3D; 3.30.450.20; PAS domain; 5.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:PSB52530.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000239157};
KW Transferase {ECO:0000313|EMBL:PSB52530.1}.
FT DOMAIN 29..102
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 103..157
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 158..195
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 231..283
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 284..330
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 362..415
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 416..486
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 490..542
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 543..613
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 859..1116
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..168
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 820..850
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1116 AA; 123192 MW; 83A009F7F402CB3E CRC64;
MQIDNISIHS ETLSPTRTGG NAPNLIEEVF RLYDRALAAT SNGITIADAT QPDKPIVYCN
PAFEQITGYD RSEIIGHNCR FLQGPDTDRA ALDQIRVALQ EQHDCKVVLK NYRKDGTPFW
NELTISPVRD SSGIVTHFIG VQSDISDRKQ AEEALKQAEE KYRSIFENAT EGIFQTSPDG
RYLSANPALA RMYGYDCPSE LIAKCSAKNL YADRTRRASF MAEIRQNGSL KEFESCVRRA
DGSTTWISEN VREVRSEAGE LLYYEGTVAE IADRKAAEAA LRDREYWLKT AIDAVPDAIN
LTDGEGRWLI ANDCALKLLG WETADYQGKT TAELAAAADP RVRDILLSWQ ETDETTWEAG
TLTSSSQIVP LPTGGSNLFE VRKVPLYNPD GSRKGMAVAG RDITQQVAAE AALRESEQRF
RAIFERGAIG MAVATLQGVA IATNPAFQAM LGRSEAELRG VDIDCCVHPE DAPASRQLRR
QLAGGDRQAY QIEKRYLRPD GSIRWGRLSA SVIDNSQGMP QFILKMVEDI TDRKQAQSAL
LQNEAKWRSL ILNSSDIITI LDASGRIVYE SPSVETVLDY EPEELIDRMI LDFIHSDDIA
AVISQQEKLI ANPADPIALE GRFRRADGSW CFLEGVGINL LADPAVNGIV VNSRDMTARR
QAEYRLSKIN ECFLGFTTDA ADNIQRLTSL AGELLGGSSA IYSHVGGGLL RAIATWQTPP
DYPAVDRAEG HICTDVCSKG GDAAVAIPDL QNTIYGKSDP AVIRYQLKSY LGQAVRLGDN
YMGVMCVLYT EPIAPTEADC KLIGIIAGAI GVEEERAAGA ARDRQKSREL QTALRELQQT
QMQLVQTEKM SSLGQVLAGI AHEINNPVGF VAGNLCHVRG YVLDLLEIVQ MYREEYPNPP
AKIQKQAEDI DLEFLAEDLP KLLNSMQTGC ERIVEIIQTL RNFSRTDEAK LKPADIHEGL
ESTLLMLNSR LKAKPNWQGI KVIKEYGELP KIKCHPGLLN QVFMNILANA MDALEESSSK
INTTTTNSSF PTITIKTETI DNKSICIRIK DNGPGIPQDH IVSLFDPFFT TKPVGKGTGL
GLSISHQIVV EKHNGKLQCL SQADKETEFI IEIPIR
//
