ID K9TSV8_9CYAN Unreviewed; 1694 AA.
AC K9TSV8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Oscil6304_5620 {ECO:0000313|EMBL:AFY85099.1};
OS Oscillatoria acuminata PCC 6304.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY85099.1, ECO:0000313|Proteomes:UP000010367};
RN [1] {ECO:0000313|EMBL:AFY85099.1, ECO:0000313|Proteomes:UP000010367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY85099.1,
RC ECO:0000313|Proteomes:UP000010367};
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 acuminata PCC 6304.";
RL Submitted (JUN-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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003607; AFY85099.1; -; Genomic_DNA.
DR STRING; 56110.Oscil6304_5620; -.
DR KEGG; oac:Oscil6304_5620; -.
DR PATRIC; fig|56110.3.peg.6903; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_241069_0_0_3; -.
DR InParanoid; K9TSV8; -.
DR OrthoDB; 5389090at2; -.
DR Proteomes; UP000010367; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 5.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 3.30.450.20; PAS domain; 7.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_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; IPR013655; PAS_fold_3.
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 NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 5.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010367}.
FT DOMAIN 148..202
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 199..241
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 270..322
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 323..366
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 475..545
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 548..596
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 683..734
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1026..1247
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1266..1393
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1417..1534
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1594..1683
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 433..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 587..614
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1320
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1466
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1633
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1694 AA; 191048 MW; D285B12B507793A3 CRC64;
MEFLKQILAF EPDIFYGYAY LWNLNGIKLH VAEALASPAM LAALAVAEGL IFLIFLYLIR
TDRPLPDPRF PKHQPPRFRE IFNSSFQFMA VLNPEGMILD VNQTALEWGE LQLEQVFGVS
FWQTPWWSGN QPSQDRLIEA IATAASGKSR RYETVIGGSG CPLRTLDFSI RPMLGQGGQV
TQLIAEGRDI TARKGYESEL LRIRKAVDSA GDAIAISDLR GHRIYQNFAC TQLFGYTRDE
MNAAGGPWML YQDPVVSQQA FETVSSGGSW QGEAEMKSKG GDCLQIAVRA DAIVDERNQI
VGFIGIYTDI TARRQLEAEL RHQETDYRQL MEQASEGIFI IDERGNYLNV NPRACEMLGY
SREELLQLNF KAIAYQPEIE IFSSPLDGLR LGENCRSEHW LRRKNNTLLP VELSAKMLPD
GRMQAIVLDI TDRKRSEAAL RKYQEQLENL VAQRTAELTR ANRQLQSEIV ARQKAQAELE
QFFKVSADLM AIASFEGYFK RVNPAITDIL GYSPDEFSRQ FSLDWVHPED RELSEEKTQQ
MLASKEAIAF ENRYRTRDGS YKWISWSAVP VPEEQSIYCV GRDISDRKSV ENALHQETRR
VTELQNRFQR LADNLPGVIY QYLITTDGTI SFPYISSGCR DILELEPEEI EQNAQLMCSL
IHPEDSQNFN ESIARSAQIL QPWKRKFRVI TPTGKIKWLQ GESRPEPQPN GDILWDGVAI
DITDLKQLEQ ELLHSEERFR TSVENMLDCF GIYSACRNER GEIIDFRREY VNASARQQYH
CSRDEMDHDC SFCQVMPDQR QSILFSKYAQ VVQTGQPLNE ELILYETEGN LGLNGMKNRP
PVREAFDIRA TKLGDGFAVV WRDISDRKQM ETAIERERQQ LQQIVNCAPV AIAMFDTQMC
YLAHSSQWLT YHGLDSFGRS KTSDNNNGTQ PSLIGRNYYQ VSSDIPERWR QAHQRALQGE
IVSVTEDLWQ KLDGSSTYIR WTISPWYLAE GEIGGIAIAI DCIDELVKAR EAALESARFK
SQFLANMSHE IRTPMNGVLG MAGLLLETPL STQQYDYAKT IRASAQHLLS IINDILDFSK
LEAGEMHLEQ FDFNLYESVE QVLDLLGAQA EAKGLDLSFL FDPNLARNLQ GDPVRLGQIL
LNLVGNAIKF TEVGEIIIQA SAIAETEETA CIRMSVKDTG IGISPEGQNK LFQSFSQVDA
STKRQYGGTG LGLAICKQLV EMMGGQIGVD SKLGEGSTFW FTAEFKKQLH FTPIEVSPPR
KLPSLRVLVV DDNPRIRQSV RELTEAWGMH TDDAANATEA WNALQQTVTL NKPYDVLLLD
LQLPSKEGLQ LLENLHYNRE QFDSHLFPET QVILMTNQSQ RDIAESLLSR GVASYFFKPV
RASRLFDTLI NVVNGPSSTA SSMGTLHAPI IPAYAINILV AEDNLINQTV ILSQLEMLGY
QPDCVTNGIE ALEAITQKTY DLVLMDCQMP VMDGYAATKE LRRREEAQRH TIVIALTANA
MRGDRQKCLD AGMDDYLSKP IEREDLAAAI RRWIHKKPGP DNCLQVPSPV KIPRIEPTAI
PSSLLTLNTA SPLPFSPPEC PVNMDRLLKV TRGNLSLQQR LLQVFIDKIP EDIEAITQAL
SNQDLAQMEH CAHRIKSAAG NVGVSSMSAI AAQLESLARQ QTLEGTAELA SQLPTILEQV
QGFFDEHFCQ KTSV
//
