ID F4XWH0_9CYAN Unreviewed; 1135 AA.
AC F4XWH0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LYNGBM3L_42570 {ECO:0000313|EMBL:EGJ31155.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ31155.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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; GL890942; EGJ31155.1; -; Genomic_DNA.
DR RefSeq; WP_008187689.1; NZ_MKZR01000001.1.
DR AlphaFoldDB; F4XWH0; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_009321_0_0_3; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EGJ31155.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EGJ31155.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1135
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003324484"
FT TRANSMEM 204..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 440..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 730..847
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 887..1013
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 399..436
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 780
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1135 AA; 128515 MW; 976A5162259182D6 CRC64;
MFSWKRAQIP LCLGAFLISV LISLLTIAPS QAQSQASKTL PPLEITQGWH YLWGDVSINN
LRNAKGCTKV EIANGNPCWQ PFSFPERLWK SQQDQQQNNV WLGVRLPDGK WQSPTLYLGA
VPNILEAYLD QQLIYTRLSP NSLPPANGEG YQWPIVPLDS NFSGKSLFIN VYVGGDKSIY
IGFFDRIVIG SKFNVIRCLF KDEISTVLGC IFILIGLWFS LTCLFRSQDK RLILAFGLLA
IAGGVYNISQ STIIPLLFKD SMNWEYTRYT AFCFLPILTL IGFEQIFGSG YFSIIQRLWQ
IHIIYSVISL GLIFIYNSSW FYERYIDHYL LLASTIILLL HAIPIAITKK NYYAKLFSFG
LSILAIAGMH DILVYRFELE NWYQRFYPWG MLLFILSLAL ILERRFAETR RLLQEYNQKL
ETKNAALQEM DQLKNEFLAN TSHELKTPLN GIIGIAESLI DGATGELSQP TSSNLSLIVS
SGKRLTQLVN DLLDFSALKH KQINLRIKPV GMREITEVVL LLSRPLVGNK KLQLINQVSS
SIPPVDADEN RLQQILYNLV GNAIKFTERG TIKVSAEVVN YYLKITVSDT GIGIPPDKLD
RIFEAFEQGD GSINRKYGGV GLGLAVTKKL VQLHGGDIDV ESTPNLGSRF SFTLPISTGK
VERKQREEVS KVQNYLAMAS DSEHLISDHL MSNHLMSNHL MSDHLMSDHL ISDHLISDQN
LSSPSMKAFK ILIVDDEPVN LQVLVNHLSL HNYKITQAVN GLDAFTKIRQ GYRPDLILLD
IMMPKMTGYE FCKKIRNKYL PNELPVVLLT AKNQISDLVA GFAAGANDYL TKPISKNELL
ARIKTHLQLA KINVAYGRFV PREFLQFLKR ESILDVQLGD YVQKEMTVLF SDIRSFTSLS
ERMSPEENFN FINGYLSRVS PVIRNYNGFI DKYIGDAVMA LFPEKADHAL NAAIEMQKQV
YLYNSHRHNS GYETIAIGIG LHKGSLILGT VGESQRMDTT VIADTVNLAS RLESLTKIYG
TEILISKPTL NYLDNRDSYH YRCLGRVKVK GKSQPVEIFE VYDANPENLI AFKSGTTPRF
EEAVAYYVEE DFAQAQQIFE ELLQINHQDR VVELYIERCA KARLFGVSEL DIVIT
//
