ID F4XPS1_9CYAN Unreviewed; 876 AA.
AC F4XPS1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LYNGBM3L_34830 {ECO:0000313|EMBL:EGJ33525.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ33525.1, 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; GL890848; EGJ33525.1; -; Genomic_DNA.
DR AlphaFoldDB; F4XPS1; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3221; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_011260_4_0_3; -.
DR OrthoDB; 569347at2; -.
DR Proteomes; UP000003959; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12974; Phosphonate-bd; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGJ33525.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EGJ33525.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 412..640
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 664..780
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 713
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 876 AA; 98784 MW; 10C622E87FD6DB6E CRC64;
MFITTCYIMI RLYFFIKSSL ILGMGLSLIP SAAPGILPPQ EPVDGTGQIT TSEVKIIKVG
VMAIRGVDHT KTKWQPTLEY LSETISGYVF QLVPLEFDTL EEIVANQEVD FVLPNPGMYV
ELEWIYGARR IATLKNLRLG KPYTQFGAVI LRHADRNDIQ DLKDLRGKTF MAVSEIAFGG
WQMAWETLLE AGVNPYRDFP ALDFGGSHDA VVYAVRDGIV DAGTVRTDTL ERMAQEGKIN
RDDFVILNQQ TQYQDTFPFA LSTKLYPEWP FSTLPHTPVE LAEEVAIALM TMPSEHPAAK
AGRYQGWTIP ANYQPCHETL RNLRVRPYED WGKVTLGQVI HQYRYWLLFA GVSCFGFSYG
LVYLAGRRRI EAQLRKANAL LEIRVEERTA EFKAAKEAAD QANHAKSQFL ANMSHELRTP
LNGVLGYAQI LQRDPQITAQ QKDQINLIYQ CGNYLLHLIN DILDLSKIEA RKMELFPREV
HLPSFLMEVV EMCRVKAQQK EIAFIYLPSS HLPDGILADA KRLRQVLINL LGNAIKFTDH
GGVTFKVEVI SKHPRLPTLQ SPLVRLRFII KDTGIGMTPE QLEKIFLPFE QVGDVDHREQ
GTGLGLAISQ TIIKLMGSAI NVESTYGKGS MFSIDLDLPI TTALIASKQA STKTIIGCHG
KARKILVVDD KWQNRSVIVN VLQPLGFELL EATNGVEGLE KATECNPDLI ITDLVMPVMD
GLEMMRRLRS LDKLKDLLII ASSASVYELD QQQSWHAGCD DFIPKPVDVA ELLEKLKQHL
QLEWVYEDFI PKPETIIDAG AEQIHLDAIV PPPSDILLQL YDLSKKGNVF DISQEAEKLE
VLDAKFVPFA KVIYKLAKDF NVKELRNFIE QYVDNI
//
