ID D8G2N9_9CYAN Unreviewed; 1122 AA.
AC D8G2N9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OSCI_3220008 {ECO:0000313|EMBL:CBN56879.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56879.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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}.
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DR EMBL; CACA01000287; CBN56879.1; -; Genomic_DNA.
DR RefSeq; WP_007356084.1; NZ_CACA01000287.1.
DR AlphaFoldDB; D8G2N9; -.
DR OrthoDB; 337251at2; -.
DR Proteomes; UP000004532; 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 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; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; 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; 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; SSF48452; TPR-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS50005; TPR; 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:UP000004532};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 364..416
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 438..672
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 712..829
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 869..995
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REPEAT 1058..1091
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT COILED 401..438
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 762
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1122 AA; 124894 MW; EE7AF3D38F2935E2 CRC64;
MSHPTRKFRL RTALVVPFVL QIVAAVGLVG YLSFRNGQKA VNNVASQLRR EVVARVQVHL
RNYLAKPHLI QQIHINTIRQ QLLDPSNFDQ MERYFWLQSQ FLDTNIGTMA FANAKGEFVG
ANKAEKYTVV ANEITGNAIR RYAVNNQGER LNLIRERPNY DARTRDWYKT AVSVGRQTWS
TIEPSALGKR LDLSAVSPFY DSTGALEGIF LTDLSLAQIS DFLHGFTIGK SGKTFVIERN
GILVASSSIK EPFILSNDGK VERLNAEKVG DTLTQKTTQY LLRQFGDLNK IDRPQQMEFL
FNGEKQFLQV SPFQDELGVL NWLVIVVVPE SDFTAEIDAN TRTSLLLCIA TLIVAIIVGI
LTARWITRPI LKVSQASAEI AAGKLEQNIE PTNIIEIEKL ANSFNSMARQ LKESFAALEK
QNEDLKDLDK LKNEFLANTS HELRTPLNGI IGIAESLIDG ATGELPQSTQ ANLTLIASSG
RRLANLVNDI LDFSKLRHNN LELRLKPLDL RAVTNVVLTL SQPLAAQKDL QLINAIAADF
PPAAADEDRL QQILHNLVGN AIKFTPIGTV TVSAEVVIGS EQLPITDSQL STANYQLAIT
VSDTGIGIPA DKFDRIFESF EQAEGSTARE YGGTGLGLAV TKQLVELHGG KINVKSQLGV
GSQFTFTLPA STVKAESTPQ INASKYNPDL ELLTSITSKN LDPKINNEKQ FKVLIVDDEP
INRQVLINNL SLYNYAITEA SNGQEALTAM ENGFIPDLIL LDLMMPQMTG YEVCQKIRAR
FPTYELPIVM LTAKNQVADI VEGFESGAND YLSKPIQKQE MLARIKTHIS LAKLTLAYSR
FVPRNFLKFL EKESIIDVQI GDQVQQEMTV MFSDIRSFTT LSESMTPQET FNFINSYLSQ
VSPVIRQHKG FIDKYIGDAI MALFPESAND AVQAAIAMQK QVAIYNKQRQ QENALPIAIG
IGLHTGNLML GTIGESERME TTVIADAVNL ASRLEGLTKL YGAGILISHN TLCCLDYSQE
QCFRFLDRVM VKGKKSAVAV FEVYDGDPAN IKQLKTQTQA RFEVAVFLYY QQQFEEAQGI
FQEVLQINPQ DKAAMLYVKR CQKYQQYGVP EGWDGVTDLD FK
//
