ID F4Y168_9CYAN Unreviewed; 1443 AA.
AC F4Y168;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LYNGBM3L_62560 {ECO:0000313|EMBL:EGJ29579.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ29579.1, 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GL890969; EGJ29579.1; -; Genomic_DNA.
DR RefSeq; WP_008189677.1; NZ_MKZR01000001.1.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_250008_0_0_3; -.
DR OrthoDB; 5522855at2; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; cd00130; PAS; 3.
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; 4.
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; IPR007895; MASE1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 360..401
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 435..487
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 527..599
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 620..672
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 915..966
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 967..1038
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1041..1091
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1109..1341
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1443 AA; 161953 MW; EDA24418288C4222 CRC64;
MIFIPKGFWQ HLTNLGLLTL VYLGLANLVH GLIGGNTLVP PVWSPAGVTQ ATVLLLREHL
WWLTEQQGVL PSVSWGQFFW TVSAQRFWPV SVITALGYIL SVLLSIGLAL LWQLRPSLER
RRDVLGFLGV SMVATLIAPT VSLTHLHLSG EFDGRNFGGM WWKWWLGDLM VVLVVVPVFL
VWCYLVKELK VGRLFAFAQR RLCRKRGQLA KVEKVEQSTQ TNLQLSNQQP LTPQASIKIK
QIILAAIWLI SLLTVSWAVF GSDIAPEMAT YPLACLTFPW LIWATLQFGQ RLTTLGCLMV
SSIAIVGTSL GTGPFLASTG DLSEAVPLLQ VFMILMATIA LFLAAITSER NSAAELLLLS
VAKYRSIFEN AVEGICQTTP DGSYISANPA LARIYGYQSP EELVASVTDI AHQLYVDPQR
RADLLLQLQE DGVVSGFEAQ IYQKDGSIIW ISKNVRAIRD SSNFLLYYEA TVEEITERKH
AQDALLYQNE RLEYQFQERT ATLRQLNRQL IAEVLEHKRI EDALRESEER FALAIQANTN
GLFEINLKTY DHYYSPQFLS LIGYPLDQDG PTINELLALI HLEDQDQVKA ILDNLCTGRS
SQRCSAVLGV SPMSDCIKKW KQKFRLLRTD GSISWILSTG LVITDDNGEV VRLVGTFTDI
TDSQRVKALL AGQNRILEMI TQWEKLPDVL DRLARLIEEQ LPKIRCAFLL VDKNGVNLRH
TAAPSLPESY IQAIDGMVIA PYMGCCGTAA YWRESVMVKD IATHPLCGSI RDLALSHNLR
ACWSIPILST QGTVLGTFST YYTEPHTPNP EEQELADKAT QLARIAIERS VAQEDVLRTN
AMLKAQQEAA IDGILVVDEN FRVVSYNHRF SDLWQTPEQL FETNDIQELL KQVSSQLKHP
EEFLAQVDYL QAHPKTTNYD ELLIKDGRIF DFYSAPVLTS GGDYYGRIFC NRDITERKLS
EAKLRQAEQK YRKLVESAGD AILMADAETG IILEANQMAE QMLGRRRAEI IGLHQSQIIP
RERFKAYSQS FQQHVEAGGV FQEELELLHQ VGTTVPVEVS ATTLELQGKT VVQGIFRDIS
DRKQAEQALK QAKVDAEVAN RAKSEFVANM SHELRTPLNG ILGYAQILQE EPNLSATQKE
QLSIIQQSGQ HLLTLLNDIL DLSKIEAIKM ELDVRDFQFP KFLEGIVEIV VISAKQKNLS
FRYEFLSPLP EFVKGDEIRL RQVLMNLLGN AVKFTDTGGV TFKVGYLGCS ELNVDRSLTE
KQGTQKMRFV IADTGIGIPP KQLAEIFLPF HQVGNTDRQV NGTGLGLSIS KRLAELMGSE
LKVKSTVGQG SIFWLDLDLP DVSQEQQGGQ GIVESTKEEK AEDVMPVAPS PEKISVLYEL
AIIGDIRGIQ EEANLIEQLD DKFIPFAQNL RQLSKGFQER QILEFVRNYM DKKDREAHGQ
SKD
//
