ID A0A0F5YJM3_9CYAN Unreviewed; 1360 AA.
AC A0A0F5YJM3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=WN50_06555 {ECO:0000313|EMBL:KKD38857.1};
OS Limnoraphis robusta CS-951.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD38857.1, ECO:0000313|Proteomes:UP000033607};
RN [1] {ECO:0000313|EMBL:KKD38857.1, ECO:0000313|Proteomes:UP000033607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-951 {ECO:0000313|EMBL:KKD38857.1,
RC ECO:0000313|Proteomes:UP000033607};
RA Willis A., Parks M., Burford M.A.;
RT "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT robusta strain CS-951.";
RL Submitted (JUN-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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKD38857.1}.
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DR EMBL; LATL02000342; KKD38857.1; -; Genomic_DNA.
DR RefSeq; WP_046277716.1; NZ_LATL02000342.1.
DR PATRIC; fig|1637645.4.peg.6708; -.
DR OrthoDB; 337251at2; -.
DR Proteomes; UP000033607; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12913; PDC1_MCP_like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 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 Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000033607};
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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 371..423
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 522..574
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 599..835
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 890..1007
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1052..1184
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 565..599
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 940
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1360 AA; 153259 MW; F4C084EBAA4C71DA CRC64;
MLIQSFHRLV SPLTRRVPLR TVLIVPFIIQ LLATVGLTGY LSWRNGQRAV NDVASQLRNE
VSKRVQLHLK DYLEKPSLIT QINNRSARLG LLSLENKQFS EYLLWEQLQL FNSVYALYFG
SESGEFVYVK RGSDGSSVAK RVEFPPERYS YRLDEQGNRS EFLEVDEYDP RQRPWYLNTL
LTERANWSKI YTFTGGELGI TASNLFYDSQ GNFRGVMGVD IILSLISDYL ENINISQNSQ
VFIVERSGLL VATSTGEEPF TMRKNDKQAQ RLAALKSPNQ LTVETTQHLL KRYEHLSRIQ
QPEQLDFQLN GERQFVQVVP YRDKLGLDWL IVVVVPEADF MSQIHANTRT TILLCIIAFG
GAIGIGILTA QWVTKPILRL NQAAKAISQG KWNYKVASSR CDEVRELAES FSCMGEQLQE
SFTVLEAKNA AMQQLNNRLI QSEARLYQFL DSLPVGVLVY DGVQDKLTFI NQTAKALFRK
EIIPDTSLDK FAQAYQLYLA GTDQLYPPKA LPLIRALKGK SLKTENIEIR HPDRVIPCEV
LAKPIYDCHG NIIYAIVVFE DITQRKEAET ERQNFTAQLK LKNEELERLD KLKDEFLANT
SHELRTPLNG MIGIAESMLE GATGTLSEQQ RKNLIMIAHS GHRLSTLVND ILDFSKLRHN
TIQLQLKPTG LREITEIVLT LSQSLTRTKK LELINTISRD LPPVKADENR LQQIFHNLIG
NAIKFTDSGY VKVSAQVINW DKDRNGTAKN YPQKRFSTEI AVTVSDTGIG IAKDKIDRIF
ESFEQADGST ARQYGGTGLG LAVTKQLVEL HGGKIWVEST INVGSNFTFT LPIAEGETAV
TLDHSSVLVH RSAVVTLENF VQSQKQNQSP QIPSNSNKNS TSNLDNNQFK ILIVDDDPIN
LQVLVNYLCL QNYTVTQASN GLEAIEILEA GYLPDLILLD VMMPRMTGYE VTRKIRETWP
PHQLPIMMLT AKNQISDLVA GLEVGANDYL SKPLNKDELL ARIKTHIRIK QLRTEKAHIR
KTFGRYVTDE VVTNLLESAE GLKLGGERRK ITMLTSDVRG FTAISERLNP EEVVKVLNFY
LSKMADVITA YQGTIDEFMG DGILVLFGAP RLRENDPERA VACAIAMQLE MESVNQQLNQ
WGLPPLEMGI GINTGEVVVG NIGSEKRTKY GVVGNQVNLT YRIESYSTGG QILISESTFN
EINSIIQVVG ENQVQPKGVK QPITIYEVGG ISGKYNLFLH QEEEIFLPLV QPISLHYTIL
EGKHIGENVF QGSIIELSAK GAKIHSRQGE QDCVPVSLTN IKLNLIWADS TMTSEDIYAK
VLEEPANIGN FYIRFTAKPP EVKIRLQRLY EHLLKQTKSC
//
