ID K9VMC6_9CYAN Unreviewed; 1315 AA.
AC K9VMC6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Osc7112_4063 {ECO:0000313|EMBL:AFZ08395.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ08395.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ08395.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ08395.1,
RC ECO:0000313|Proteomes:UP000010478};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-2012) 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}.
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DR EMBL; CP003614; AFZ08395.1; -; Genomic_DNA.
DR STRING; 179408.Osc7112_4063; -.
DR KEGG; oni:Osc7112_4063; -.
DR PATRIC; fig|179408.3.peg.5004; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_10_3; -.
DR OrthoDB; 567946at2; -.
DR Proteomes; UP000010478; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd12913; PDC1_MCP_like; 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; 6.10.340.10; -; 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; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ08395.1};
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:UP000010478};
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 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 373..425
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 506..560
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 601..628
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 653..703
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 704..741
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 779..831
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 849..1080
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1106..1222
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 687..714
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1155
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1315 AA; 147028 MW; 346ED44EFE73AE61 CRC64;
MFPKPLNRLA TKIIGKVPLQ TVLVVPFLVQ IVGTVGVVGW LSFQNGQRAV NDVAAQLRGE
ISDRIKDRME HYMSIPHIVN HLNLQAIKLG QLNLEDKQKL EHHFLEQIQY FDSISIIYTG
KENGEHSGAI RTKDGTLISA ADSSTGNKLA RYTADSQGNR VQLVQISPNI YDPRTRPWYI
AAAAKKKPIW TPIYTDFLTR ELAITAALPI YDDAGKLLGV AGSDLLFSRI KEFLVSLKIG
KSGQTFVMER SGMLIATSTA SPEFVVEGKE IRRIKASESE NPVIRQTAQH LDKSYDSLAK
ITNSQQLTFD VDGKRNFIQV APFKDDRGLD WLIVVVVPES DFMEQINLNT RTTFLLSLAA
LMGATILGIL TAKWVVQPIL RLNAAAKALA RNEWDTKLTL NREDELGELA TAFNSMAEQL
QHSFNSLSES ESRVKQFFNA VPLGIFIAEP NGQPHYINPT GEQLLSQGIV PADSETLRQA
YRVYLAGTQE IYPAERDPIL NALQGKSVTV DDIEISATDK TIPLQVWGTP IYDAQGNIIY
AMCAFQDITE RKQAEKVLKE YNDNLAVQVA ERTADLAKAK EKFSKAFRLS PNAITLTRIS
DGRHIEANES FCRMMGYSHE EIIGKTAVQL NFWASLGERD RMIQMLKNKT AIHNYELRFR
NKNGTERTAL LSIETIDIEG EACFLSISSD ITERQKAETA LREAEEKYRN IYENALNGIF
QTAIDGKYIS ANPALANIYG YDSPADLIAA QPNFNNQLYV KPNRRDEFAA LMNEYGILSN
FESEIYRKDG SIIWISENCR AVCDEAGNLL YYEGFIKDIT DNKQAEIKMQ QAKEAAEAAN
KAKSTFLANM SHELRSPLNA IIGFAQVMIR SKTLSPENQE DVAIILRSGE HLLALINQVL
DLSKIEAGRT TINEKNFDLY QLIDDLEDMF ALKAEQKGLQ LIFDRDAEVP HYICTDEVKL
RQVLINLLNN AIKFTSEGGV SMQVKGGRRN IHNKNSTDQL PGRYWLHFEV QDTGTGIAAE
EIHQLFEAFV QTKTGKDSQE GTGLGLAISR QFVQLMGGEI TVSSEIGKGA VFQFDIQVNL
VEATDIESKK TQRRVVALEP NQPSYRLLIV DDKPLNRQLL VKLLSPLGFE LREANNGKEA
VDIFMEWEPH LIWMDMRMPV MDGYEATKQI KTTTGGQATA IVALTASVLE EERAVILSAG
CDDFMRKPFR EEDIFVAMGK HLGVRYIYEY PTAVSAAGVE DSSQEVLTPE AFASVSPDWI
AEFKQSILSV DMEAIASSIA QIGTVNPSLA GKLQDCINNF EYDRILNIID LSEKQ
//
