ID K9PRA5_9CYAN Unreviewed; 1854 AA.
AC K9PRA5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cal7507_4735 {ECO:0000313|EMBL:AFY35092.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY35092.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY35092.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY35092.1,
RC ECO:0000313|Proteomes:UP000010390};
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., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; CP003943; AFY35092.1; -; Genomic_DNA.
DR RefSeq; WP_015130889.1; NC_019682.1.
DR STRING; 99598.Cal7507_4735; -.
DR KEGG; calo:Cal7507_4735; -.
DR PATRIC; fig|99598.3.peg.5321; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_34_0_3; -.
DR OrthoDB; 517727at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFY35092.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW Transferase {ECO:0000313|EMBL:AFY35092.1}.
FT DOMAIN 14..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1601..1854
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1533..1592
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1854 AA; 209159 MW; 5BA55F739AB5196C CRC64;
MTVLLDTTYT ILGYRITEKI YSGSKTLVYR AIREEDQQSV ILKLMRNEYP TFAEIAQFRN
QYTITKNLDL PGIIKPHNLE NYQNGYALVM EDFGGISLAD WQLEKKPVSL SEFFAIAIQI
VSILERLHRD RVIHKDIKPA NILIQPTTGE IKIIDFSIAS LLPREIQFLT NPNVLEGTLA
YISPEQTGRM NRGIDYRTDF YSLGVTFFEL LTGQVPFSAD DPMELVHCHI AKEPPQASSI
NTNIPSILSD IISKLMAKNA EDRYQSSYGL KYDLELCYDQ WQNTGTATFE LAVQDISDSF
LIPEKLYGRQ RELETLLAAF KRVTEGTTEM ILVSGFSGIG KTAVINEVHK PIARQRSYFI
KGKFDQFQRD IPLSGLVQAF RDLIGQLLSE TDAQVQQWKA RILSALGTQS QVITDVIPEL
ELIVGKQPEI TELSGSAAQN RFNLLFQRFI QVFTTKEHPL VIFLDDLQWA DVTSLKFMQL
LMCENTSSPF AGELQKLGKP PGGLLLIGAY RDNEVSPVHP LSLTLKEIKE TGTIISSINL
KPLSQSDLNH LIADALRCQE LLAVPLTQMV FAKTKGNPFF TNQFLKSLHK DGIITFDFDV
NYWRYDISQL QVLALTDDVV EFMALQIERL PNITQEVLKL AACIGNEFDL KTLAIVHEKS
AGDTATDLWT ALHEGLIIPQ TDVYKLFQDS HVSVGVIDSK NPEQLPFNSV SFPKYKFIHD
RVQQAAYSLI PEDKRKPIHL KIGLLLLNNI PVAEREDKIF ELVNQFNIAV EFITHQTKRD
ELAAMNLIAG RKALVSTAYL SAVKYLTTGI ELLADNSWGK KYELTLDLYE TAAEAAYLAG
NFEQMDQFVE VVLEQAKTLL EKVKVCEVKI QAYGAQNKAL EAVNTALAFL KLLGVEFPDN
PAQYDVQLAM REIASNLNGR CIEDLIDLPE MIEGKSLAAT LLLSSVSGLV YQAVPQLFPL
IVFKQIKLSL THGNTALSAF AYITYGLILC GVVGDIESGY QFGKLAINIM DKYDTKKVKA
KIMQGFNAVI RHWKEHTREI VKPLLEAYHT GLETGDLEYA AFSLKGYSYS SYFIGKELTQ
LEREMVTNSN AITKIKQDRA FNWNSIFRQI VLNLLGNVEN PCYLIGESYN EDKMLAIHLQ
AKDGVGLLYL YFGKLHLCYL FQNFHEAIKN AAIVQNYIDC GIGQLFVPVL DFYDSLTRLA
IYPNVDEYEQ KEILKKVANN QEKMQHWAHH APMNYLHKFY LVEAERHRVF SQYLEAIELY
DRSISLAKEN EYINEEALAN ELAARFYLEW GKPKIAQTYL TDAYYCYSRW GAKAKVEDLA
KRYPQLLAPI LKQEKLSLHP SEKSTYSHSK SLSSVSNQQT IIGSKTSISD SLDLASVIKA
SQALSGEIEL EQLISTLMKV VMENAGASKG ALILTKGNNL NLKLTAVSAN STTEFPAINL
ESSDDVPITL INYVKRTLEI LVIDDAKADI SLAEDSYIIR KQPKSLLCIP IINQNKMLGI
IYLENNLTTG AFTRDRVELL KLLTTQVAIS LENAILYKNL AEANENLEEY NHKLEDKVQE
RTHELNEKNQ HLQQAIEELQ RTQTQLIQSE KMSSLGQMVA GIAHEINNPI NFIHGNVSHA
SEYVKDLLDL IDIYQQEYPQ PSSLVEAKNE EIDIDFLLED LPKLLDSMKM GSSRIRNIVL
GLRNFSRLDE SEMKPVDIHE GIDNTLMILQ HKLNQQSHRP EIEVIKEYGQ LPEISCYAGQ
LNQVFMNILS NAIDALEETF ISGKKTDNLT IRLHTELVDN HTVKIQIADN GSGMTEAVRQ
KIFDPFFTTK PIGSGTGLGL SISYQVVVDK HKGKLTCDSA LGEGTEFVIE IPMN
//
