ID A0A1J1LT62_9CYAN Unreviewed; 1452 AA.
AC A0A1J1LT62;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PL9214650459 {ECO:0000313|EMBL:CUR35020.1};
OS Planktothrix tepida PCC 9214.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=671072 {ECO:0000313|EMBL:CUR35020.1, ECO:0000313|Proteomes:UP000184315};
RN [1] {ECO:0000313|Proteomes:UP000184315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Regsiter A., william w.;
RL Submitted (OCT-2015) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CZDF01000172; CUR35020.1; -; Genomic_DNA.
DR RefSeq; WP_072721915.1; NZ_LN889813.1.
DR STRING; 671072.PL9214650459; -.
DR OrthoDB; 5389090at2; -.
DR Proteomes; UP000184315; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CUR35020.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..196
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 314..366
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 403..455
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 473..516
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 529..583
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 788..1013
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1033..1150
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1177..1294
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1354..1447
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 751..788
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1083
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1226
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1393
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1452 AA; 163779 MW; BE3F9DCFFBFC1589 CRC64;
MNIFNKILNK IGWIPLLTGT GISAATLLLW SSLITQERHQ IQQLLHQEAV TVELIIYNQI
TSRIQGLERM VVRWEVRGGI PKNEWESDAK NYFEDYGGFQ AIQWVDSKFN VRWIYPLKGN
EAALNFNLEH DILHHPSLER ALNSNQTALT PAITLVQGSE GFVAYLPIFN RKNNKFQGFI
VGVLQVKSLM NLILKSENLK YYIVDILQNN EIIYRYQTNP LIHPIQQKYI KKLDLYGTEF
DLVIIGSSEL IQLIKSPLQM VILWGGFMMA LSLTLTLYFA RSSLRKSRQL EEINQKLIQQ
ICKEEATRQI LEETTTLQEA ILNSANYTIL STTIDGTIRT FNKTAEQLLG YSAEAIIGQK
TPEIIHDPEE VKHRALLLSQ ELGTTIELGF EVLVAKALQG DIDEREWSYL RQDGSRFPVL
VSITSLRNQE GEITGFLAIG NDITERKRSE EALQKTLREL AFHKFALDQA AIVSMTDGKG
NITYVNERFC KISGYSKDEL ISHTHRVVNS HYHPSEFFAH LWSTIHQGKV WQGEIKNQCK
SGQFYWVDTT IVPFLDIANN PFQYLAIHFD ITQIKEAEEQ LKQQIKQAIL LKTITEEIRQ
SLNTKRIVET TAQLLGQTFE VNRCLIHTYL EPPVSELPVV AEYLVGGYPT LMGVKISIQE
NLYTEQLIIQ DQAMATSNVY TDPLLATLKV FCRHIKLKSV LAVRTSYKGK PNGVITLHQC
DRFRDWTEDE IELLEAVAAQ VGIALAQGKI LEQEIRQGEQ LSQQNLALEK AKAEAEAANR
AKSEFLAMMS HEIRTPLNAV IGMTGLLLDM NLTDQQHEFV ETIRTSSDTL LMVINDILDF
SKIESGQLDL EKHPFNLRNC VEEALDLVAS IAHHKNLELA YLITPSTPTT LIGDVTRIRQ
IIVNLLSNAV KFTETGEVII SIDAELIEEE NSTHFYELHF AIKDTGIGIP EERRERLFKP
FSQVDSSMTR RYGGTGLGLV ISKRLCEMMQ GKIWVESTLN VGSTFHVKVI LQSDPNASIS
DVEKVSLDLS HKQLLIVDDN ATNRQILTLQ AQSWGMEVQA VESGLEALTL LVQNTAFDLI
IIDMQMPQMD GLSLANCIHA LPNTQHLSLI LLSSVGNFLP QDVATQHLFA ASLTKPIKQS
QLYNTLAQVL THKQTPVQPF PTLTPLYPPL AETLSLRILL VEDVPVNQMV ALKMLQRLGY
RADVANNGLE AIDSLQRQPY DLVFMDVQMP ELDGLETTRY ICKEWPTVSR PWIIAMTAHA
MQGDQEECLN AGMNDYISKP IRMTTLIEAL ERYKTSRITV PNSEVSSQKK NDVPGHLSLV
TKDYLLPQIH NPIVDHCLDQ ETINSLRLMA GEDADVMLVE VFNSYLEDAP QRLQAIQEAI
TNQGALALQK SAHALKSLSV TVGAVHLAEL AGELEVKGRT GSVGSVQSLM EQLVQEYEQV
KVALQDEITR IQ
//
