ID K9Q5D0_9NOSO Unreviewed; 1685 AA.
AC K9Q5D0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Nos7107_0214 {ECO:0000313|EMBL:AFY40900.1};
OS Nostoc sp. PCC 7107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY40900.1, ECO:0000313|Proteomes:UP000010381};
RN [1] {ECO:0000313|EMBL:AFY40900.1, ECO:0000313|Proteomes:UP000010381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY40900.1,
RC ECO:0000313|Proteomes:UP000010381};
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 genome of Nostoc sp. PCC 7107.";
RL Submitted (AUG-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; CP003548; AFY40900.1; -; Genomic_DNA.
DR RefSeq; WP_015111142.1; NC_019676.1.
DR STRING; 317936.Nos7107_0214; -.
DR KEGG; nos:Nos7107_0214; -.
DR PATRIC; fig|317936.3.peg.229; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_000445_114_15_3; -.
DR InParanoid; K9Q5D0; -.
DR Proteomes; UP000010381; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 3.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 5.
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; SSF55781; GAF domain-like; 3.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFY40900.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010381};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFY40900.1};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..384
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 385..457
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 816..886
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 890..942
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1320..1538
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1564..1682
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 234..261
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1613
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1685 AA; 186215 MW; EB3D87A66910BF09 CRC64;
MPYIPYSQLL RYGFVVVIVA TALVIMLLLD PLLDMKGTPF LLFFSAVMMS AWYGGLKAGL
LATFLSVIVS DYFFLSEHYA LSLSLSNGVK ILLFAVQGLL FSFLCEELRH AKRKAEINLQ
KFKISEERFR VALSNSDIVV FQQDRNFRYQ WVHNLQGIDK AEALLGKTDD ELFPVAIAQQ
LTAIKRRAIE QDISAREEVC VILRGKVLYY DLLVEPLTGI DGGVTCVGVN ITERKQTELE
KAKLQSQLQQ ALQQKDESLA LLNAWLMSSP MALAFLDTEL RYVYANEALA AINGVPQNQH
IGRTLPEVLP EWASQLEPIF QELMITKQPL LNQEISGETY PSGVYRYGLV SYYPVSLPDG
QLLGVGITGV DITPVKKAEQ ALRESEAKFR SVVESNMIGI GFWEGDGRIT DANEALLKML
GYSRQELVEK KLDWRNLTPV EYRRLDEQAL TQFQENSFCT PYEKEYIRKD GSRFQVLVGG
SCYEGTLERG AFFVIDITER KQAEDKLRYI AEISSLLSTS LDYEETLQQI AKISVPQLAD
WCIVDILEED GSIRRLPVVY TDPFQAKLAQ KLQEYVPNAQ GTHLIARVLQ TAIPKLIAEV
SDSVLIAATQ NEEHLEIVRQ MGLKSVIVVP LIAHQRVLGC ISFAIAHRCY DQADLNLAID
IAYRAALAVE NAQLYRDNHQ ALINYAESLL LLDALLAGAP VAVCFLDREL RYVRINQVLA
DINGFPIEAH LGRKFGDIFS SMATQFEAQL QQVLETGEPL LNVEISGEMP GKPGVYGYWL
GNYYPVRNAL DETVGIGIML SDVTATKVAE VALRESESRF RAMFNQAAVG IALVALNGKF
LQVNPALCDI TGYSQEELIQ MSFQDITHPD DLAIDWEQAG RVLTKEISGY SLEKRYIRKD
GSVVWVNLTS SAVWDIHGQA KYAVGIIEDI SERQAALRDR QQAELAQTFL VEASSLLAAS
LDCQVTLNNV ASLLVPTLAD WCVVDVLGEN DVIEQIAMIS ANLVQKERLT ELRRRYPPRY
ENNSPFRETL LNKQSVFYPE LPDQILAQMA EDEEHLKLLQ SLGMNSLMII PLHLRGKVFG
VISLVRTASS SAYNSADLAL AEDLAHRAAT AIDNARLYQK TQQAKQAAEL AVSRTVRLQK
ITAALSEAIT PQQVADVVVN QGIAALGASA GSVSLLAEKG SCLKVVQATG YPSSVLDAWK
SFSVTAAVPL AAAVRTGTPI FIESPAAFAA NYPHLAELPS VTGNSAFACI PLILEKQVIG
ALGLSFSHTQ IFSEADQGFM LTLGQQCAQA IARAQLYEAE RHARSEAETA NRIKDEFLAV
LSHELRTPLN PILGWAKLLR TRKNDEATIV RALETIERNA KLQAQLIEDL LDVSRILRGK
LSLHIRTVDL NSTMTAALET VRLAAEAKSI QLQTVLPQHK VEVMGDGDRL QQIVWNLVSN
AVKFTPAEGR VEVRLAQVGM EAQIQVIDNG KGITPEFLPY VFEYFRQADG KTTRVFGGLG
LGLAIVRHLV ELHGGTVFAD SPGEEQGAIF TVRLPLHKST ESVSTANSVQ MDLATQDSLL
AGVRILFVDD QADVLEFFSF ALEQYGAEVT AVASAAEALE ALVKLQPDIL LSDIGMPIMD
GYMLLRQVRQ LPPDKGGEIP AIALTAYAGE IDYKQAMAAG FQRHIPKPVD PLDLAMAIVQ
LISQK
//
