ID F4XJZ7_9CYAN Unreviewed; 1754 AA.
AC F4XJZ7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-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_09080 {ECO:0000313|EMBL:EGJ34956.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ34956.1, 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; GL890825; EGJ34956.1; -; Genomic_DNA.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR HOGENOM; CLU_000445_34_2_3; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 9..272
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1518..1734
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1754 AA; 197327 MW; DF953D837DA3CB41 CRC64;
MLQFPNYQIK LLEELEAGVS TVVYRGYHQQ QQRPVIIKLI KSDYPSLKEI SSLRQEYTIS
QAIDCEGIVK CYGLENDNNG LALIFEDFGG QSLKHLINSH TMTIKDFLRI AISLVETLDE
LHKVPIIHKD INPSNIIINP ETGQVKITDL GIASRLSLEN PTTSNPNWLE GTLAYISPEQ
TGRMNRSIDY RSDFYSLGAT FYEMLTDRVP FITTDPMELI HHHLAQYPVP PHQLNPEISE
VVSLIVMKLL RKNAEDRYQS AAGLKVDLET CLSQLQTTGK IETFTPGTYD IGSRLLIPQK
LYGREGEVAT LMEAFERVSV GATELMLVSG YSGIGKTSVV NEVHKPIVKA RGYFISGKFD
QFKRNSPYAA LLEAFRGLIR QLLTEPAQTL GIWKQNLLHA LGANGKVIID VIPEVELIIG
EQPEVPQLGA SESQNRFLRV FQQFIGVFAQ PQHPLVLFLD DLQWADLASL TLLQTLMTNC
DRNYLLIIGA YRDNEVSPTH PLIQTIEKIQ ETDSVIDQIK IEPLRKQYVQ QLVADTLNDT
QGKNQTKPLA ELLFHKTQGN PFFLTQLLKT LYSENLLSYD VTSGSWQWDI DQIQAIGITD
YNVVELIARS IGKLQETTQQ VLKLAACLGN QFNLEMLAIV NEDSTIITAT QLWEALQIGL
ILPLSDSYKI PLLFEQEESA DFGLSDVKVN YKFLHDRVQQ AAYSLIPESD QQATHLKIGK
LLLNHTTPEA REENIFALVN QLNFGTDLLT AQWEKDELAQ LNLIAGQKAK AAAAYASALK
YLNVGLGLLP ADTWTDNYDF TLALYLEVVE AEYLNSNFDQ SNLLARVALE QAKTQLDQVK
VYELKIHGYI AQNQMQVALD TGLQVLDMLG IPLEQDPPKD LISEDLADLP EMTDLTKLAA
MGILKSVGTP AFVANPALYP LLIFTQINLC INHGNSHLST DTYINYAMIL CGFMGDIDGG
YKFGQLSLML LEQFDAKELK SIVLDMFNGH IRHWKEHLKE TLNPLLEAFN SGLETGELTY
SGFAALNYCT NLLFVGDDLD LAAQKYGQYL EWLQKRKLDY HVIYGQIGKQ LTLNLLGKSD
DPCQLIGEDF NELEMLPILR EQNNGTSLFY LYLAKSILFY WFKQPEQAIA QARAAEQYAQ
SVAGLILVAE HNFYYSLALL AHYPHVEPQQ QGEYLTEVAA NQETLKTWAY HAPSNFKHKY
ELVEAEKARV LGQHWQAMER YDQGIEGAAD QDYIQEEALA NELAAEFYLS CGKRKIAQAY
LTDAYYGYSR WGALAKVRDL ESRYPQLLSK ITAQPTTKVP LDSITNSTIA VSLNALDLSD
VIKASQAISE EIVFENLLDK LMQILLTNAG AKKGFIILSK DDKLIIEAAG TVVNNGVTFR
ESIPVTITQH LPISVINYVA ITKENLLLNN LVNNSTFADD IYIINNQPKS AVCLPLLRKN
NLIGMVYLEN NMVSGNFTNE HLEVLSLLCN QAAISLENAT LYQTLHEVQV RERLEKQIRK
SLEREKELTE LKSRFISMTS HEFRTPLTTI MGVTEIFKYY SQNWTDEKKQ NYLDRIQVNV
KHMLHMLDDV LVVNKANAGK LKFNPAPLNL LEFCRDLVED IELGIDTQQS IVFSIQCECP
EVNFDEKLLR HILINLLSNA TKYSPNDSTI NFDLICQQEE VIFKIKDQGI GIPEEDQKQL
FESFHRCNNV GNIPGTGLGL AIVKQSVEVH GGEITVNSQV GIGTTFTVTI PLYSPAVPEQ
VQRPRAVCQL AVGS
//
