ID A0A0C1UND2_9CYAN Unreviewed; 1796 AA.
AC A0A0C1UND2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=QQ91_006010 {ECO:0000313|EMBL:NEV66665.1};
OS Lyngbya confervoides BDU141951.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=1574623 {ECO:0000313|EMBL:NEV66665.1, ECO:0000313|Proteomes:UP000031561};
RN [1] {ECO:0000313|EMBL:NEV66665.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV66665.1};
RA Malar M.C., Sen D., Tripathy S.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NEV66665.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV66665.1};
RX PubMed=25745003;
RA Chandrababunaidu M.M., Sen D., Tripathy S.;
RT "Draft Genome Sequence of Filamentous Marine Cyanobacterium Lyngbya
RT confervoides Strain BDU141951.";
RL Genome Announc. 3:e00066-e00015(2015).
RN [3] {ECO:0000313|EMBL:NEV66665.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV66665.1};
RA Sarangi A.N., Ghosh S., Mukherjee M., Tripathy S.;
RL Submitted (FEB-2020) 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 -!- 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:NEV66665.1}.
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DR EMBL; JTHE02000003; NEV66665.1; -; Genomic_DNA.
DR Proteomes; UP000031561; Unassembled WGS sequence.
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; cd16916; HATPase_CheA-like; 1.
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;
SQ SEQUENCE 1796 AA; 191551 MW; 01FFD9A7FFC974D8 CRC64;
MMPEQQQRIL GYFIEEAKDH LNTIEQGLLN LQSTIQDPEM VTEVFRAAHS VKGGAAMLSL
GSIQATSHRL EDYFKLLKEA PTTQIDRDLE TMFLQVFDGL QALLEELQGP FGLTEEKAQE
VMADIEPVFD DLESHLNELI AAAPAAAPAA AATAPAPAQA TRTVASSSED SALKLVFSSD
VPGHLREMLT LFKQVDTEAS RSALQACCDA LKRVGEQFDL SLWCDLTTAA RHAVGNSDQT
YRSLAPVIIK ELKRAQEQVL SGQANAIVVS AELESLMPLL VETEDVVGDI DSLLDDALST
TEEPDLADLF ATETESATGA EADLDWLDFS EDAADTAASS SDDDLADSLS ALTNDDSQAE
LPREPTVGTA ELNSLADLFE GEVSELDSPW EEISESEAAV ADTPSPDIEL DSDFSDLLDG
SLGEDDDADS SGDLADLFGD NSNFGDAEVA VSSEADDDLD DLLNLGEEPS DAEAVATETD
DSGLDSLLDG LEATTEDGSN DLGDDLDLGL DESSSEELEF AASPADVGTD IDDFDDLFGG
ETTVSETVDE VSEASLEFDA GDHDAALESA AASDTAPSTE IDDFGAIADP WSTGSDDSTS
DDTELALGAL DDWSDETAPA SASSDSASSD LDFSDFPEID ETDAATQEDE ADDFDDLFGT
AAASDASSVT DAAAGADATT PAADSDLSSL FAGDAPTDDT DLDFLDETAS DTSSLVGDEN
FLFDEETGSA AGSDETDLDD LLDEATIPSE AATTLPDVSD AASDDFDLTF ADDSDEALAL
ENDTAAIEAE GGDSATPDDS DDLFGEDTSA DDSDDLFGTA DVELMDTGVA SSGDDTDDFF
GSDDVSSSDA EVTVAAPSDD IDDFFSTDES AVEVASTNTE DATVGIGTDL AGAVSDADDA
SDASAPLLDF DTDSGSDDVD LELAPESDSQ ETAAIDDSDF DDLGLAESGL EDSELEDLGA
EVEASDLFDE SGDSAVDNDL GELDLDLDAS EDAADGSLGL DDLNLDGDDE SGFDDLDAML
ADDDADEATE SLALDELAVS SDDEFGDLDA LLDDDAAAPV PTAAAELDVD FDELDALIGD
TDAPATVAIT DDGGEPASDE FGDLEKLLEE ADQTLGGGST SMRSPGPGRS TRRVGGIVDQ
TMRVSVKHLD NLNNLVGELV VNRNSLEQDQ DRFRQFLDNL LFQVQQLNDV GQRMRDLYER
SLLESSLLAS RQAFHAGGSV FSTTTNGSNG DSHATGASFD ALEMDRFTGF HTLTQEMIEL
IVRVRESSSD IAYTVESTDQ IARQFRQVTT QLQEGLNKAR MVPFAQTADR LPRAVRDISI
KCGKEARLVV EGRETLIDKM LLERLYDPMT HLVNNAITHG IEPPEERAAL GKPREGKISV
RAFYQGNQTV IYIEDDGAGI NPDVLKRKAI QKGLITQAEA DRMNKLETYE LIFHHGFTTR
DQADDFAGRG VGMDVVRSAL SEIRGSINID SELGKGTSFT IRLPLTLSIS KALSCLNNQA
RIAFPMDGVE DMFDVPRERV QTNEEGQSFI QWRDMSLTFQ PLSDLLQFNR SLGRGRVYGG
SQDDDMVSIV VLRNANTYIG IQVDRVLGEQ EIVIKQIEGP VPKPMGIAGA TVLGDGRVMP
IGDVLELIDI AQGRVRREAG SSIWAQVELP PEEDAAPVKA EPTVLIVDDS ITVRELLSMS
FNKVGYRVEQ ARDGQEAWEK MRSGLPCDLV FCDIEMPRMD GLELLSRMQK DSMLKNIPIA
MLTSRGADRH RQMAVDLGAS GYFTKPYLEE ALLEAAQKML QGEVLIGAGA GAEEAE
//