ID K9VCW1_9CYAN Unreviewed; 936 AA.
AC K9VCW1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Osc7112_1227 {ECO:0000313|EMBL:AFZ05771.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ05771.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ05771.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ05771.1,
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};
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DR EMBL; CP003614; AFZ05771.1; -; Genomic_DNA.
DR RefSeq; WP_015175095.1; NC_019729.1.
DR AlphaFoldDB; K9VCW1; -.
DR STRING; 179408.Osc7112_1227; -.
DR KEGG; oni:Osc7112_1227; -.
DR PATRIC; fig|179408.3.peg.1492; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_2_1_3; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000010478; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFZ05771.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010478};
KW Transferase {ECO:0000313|EMBL:AFZ05771.1}.
FT DOMAIN 2..110
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 405..647
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 649..791
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 814..931
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 262..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 864
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 936 AA; 103344 MW; 42DD7665CC2B2F82 CRC64;
MNDDDLNELI DAFTAECEEF LQSMETNLLA MEAAGLKERQ AAVKEMFRAA HSIKGAGSML
GFQNVSAAAH RLEDCFVILR DRTDLSALEP TTVSVLLQGV DALKKITIES VQHSDVTTPD
QTENLEAIAQ IFAQFQAKYG KSEQPSVPAV SQSAAPETLK LIFEHQVPAL FNRLETELSQ
ASEADLAQSV TALNQVYYQL SGLAGMLQLP DFGKVAAALR DLIDSPDLTL QRLQSDGWAI
AQNLQTARQQ ILEGRAIDIP EISPTPTLPL SPTPTPPEIS PSPTVPPSST LPVPNPQRPT
IRVDLERLTE LVNLVGELVI NRTNLELQES ELRDEVKRIR RNIVDLSQFG GQLREEYDRL
SFADWRGGNG NSGLRKLAAA ETESPMIASG KSSPVHAHFD ILEMDRYTEF HSTAAEVIET
AQAISQSATK LDTLAMKFER STDQLRRITE QLRSRVMQLR VVSFSRAVDH LPRALREMCL
TYDKEVNLLL VGRDTKIDES LLDALRDPLI HLVRNAFDHG IEMPEVRKAS GKPASGQIEI
EARHQGGQTI ITVADDGKGI DPEMIRRKIV TKGLATEEQA QEFSIAELYD FLFWPGFSTT
EGVSDLSGRG VGLDVVRTNL RTVRGTVKVD SRLGKGTSFI IKLPLLLSIT DALMVKTDHN
KIAVPLDAVE EILHIKASEV HIAGNQPMLW WREEFIRLVR MQDLLEYSVL PPDAPSPDPL
TQEEIPVLVL ASTEGMLAVA VERLIGQQEI VVKPLPPPLS KPRGVLGTTI LGDGRVVNIL
DVDDLVGQPV VNSSIAAVSG KVHEIPPSSS KSPQILVVDD SYTIRQLLSL TLTRARYRVV
QAKDGLDALE KLQNGLDCSL AIVDIEMPRM DGFELLRSIR STERFAKIPV AMLTSRSGEK
HRQMAMELGA NKYFTKPYSE AQLLQAIPKL IHHSRI
//
