ID K9V4N6_9CYAN Unreviewed; 1958 AA.
AC K9V4N6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cal6303_3884 {ECO:0000313|EMBL:AFZ02801.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ02801.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ02801.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ02801.1,
RC ECO:0000313|Proteomes:UP000010477};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-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; CP003610; AFZ02801.1; -; Genomic_DNA.
DR RefSeq; WP_015199426.1; NC_019751.1.
DR STRING; 1170562.Cal6303_3884; -.
DR KEGG; calt:Cal6303_3884; -.
DR PATRIC; fig|1170562.3.peg.4236; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_34_1_3; -.
DR OrthoDB; 573511at2; -.
DR Proteomes; UP000010477; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:UniProt.
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; cd00130; PAS; 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; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR000595; cNMP-bd_dom.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF08447; PAS_3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000313|EMBL:AFZ02801.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:AFZ02801.1}.
FT DOMAIN 11..275
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 945..985
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REPEAT 1216..1249
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1530..1606
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1609..1660
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1701..1958
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1510..1540
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1646..1692
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1958 AA; 220934 MW; 8A8DF218D5703AE8 CRC64;
MLTTQVNIPG YQVDKQIYNG CKTIVYRGYR ESDSLPVAIK LLKNPYPTFS ELVQFRNQYT
IAKNINSSLI LQTYSLETYK NSYILIMEDF GGISLNQWEG KEKISANLVD FLQIAIALTD
ALDILYRHNI IHKDIKPANI LINPDTKKIK LIDFSIASLL PRETQIPTNP HGLEGTLEYL
SPEQTGRMNR GIDYRTDFYS LGVTFYELLT GGLPFQSDDP LQLVHCHIAK QPPHTAHNGE
IPQVLWDIIM KLMAKNAEDR YQSALGLKCD LENCLSQIKE AGKIEDFKIA QWDLCDRFII
SDKLYGREAE IATLLTAFER VTCGATEIML VAGFSGIGKT AIVNEIHKPI IQQQGYFVQG
KFDQFNHNIP LSAFVQALRD LMRQLLSESD SKIEYWKSQI LSAIGNNGQV IIEVIPELEQ
IIGSQPIVPQ LSTNAAQNRL NLLFQKLIAI FTRKEHPLTI FFDDLQWADS TSLNLIKLLT
TEITPGYLFI IGAFRNNEVS SNHPLICTLN EIKNAGITIN TITLLPLSVS DNNRLIADAL
KCTLEESLDL TKFIYQKTQG NPFFNNQFLK SLKENGSITF NMDAKAWEFD INQIYTLDLN
DDVVDLIVTQ LKNLPQSTQN SLKLAACIGT SFKLKILSII TEKSQIDTAN DLWQALKEGF
ILPRNEASKF SQSNIVQDNN KLDNIFIFED CEYKFLYDRV QQAAYSLIPE EEKPATHLKI
GQLIIENNSP ENCQENIFEI VNQLNIGRAL INQESEREQL IILNLTAVRK AKAATAYSAA
SNYLAICIEL LPFDSWNSHY DLTLKLYEEA VEIAYLNADY QLMEEMIEIV LSQAKTLIDK
IKVYETKILA IKAKSQLRES IEVGLELLKL LDVEFSKQPT SEDIGEALTE TLLAWKEISI
PSLLGAKEMS DPIKLAAMRI LTQLTPSAYQ AFPSLMPLLI FKQIIFIIAE GNCPISAFSY
ADYGLVLCGI VGDLDAGYKF GELALNIIDR FQGDFYKCRT YFIVYSHIHH WKSPLSASLP
FFLEAYQVGL AHGDLESSAL NAQMYCCHAY FVGKELVALA SEMDIYRQAV EELKQQGALT
SLEICQQTVL NLLGHSDDPC QLVGDIYDEN ESLPLLKTLH NRAAIYHLYY HKTVISYLLG
KYQQAAFYAS LVESYADIMP AAFTIPLFNF YNSLLSLQLY TYAETKQEKN NYLKKVVTNQ
RQLKQWSNSA PMNHLHKFYL VEAEYHQLLA NYQEAIEYYD RAIRLAQENK YIQDEALANE
LAAKFYLTWG KERIAQSYII DAYYCYVHWG AKVKIEDLEQ RYPQLLAPIL QKQQQSLNAN
EIIPIASFHS SKAATLGINS ISETLDLATI IKASQTLSRE IELDKLLIAL LEVLLENAGA
DKCVLLLPKN EQWVIEGICQ LGQSPIVLQS IPMQLGQYLP ISLINSVKHS LKASVIFNAV
AHANLAVDPY VLHQRPKSVL CTPILNQGKL VGILYLENSL TTGAFTSDRL ELLNLICTQA
AIALENARTY QQAQNYGKQL EQSLEALNAS EARFQKLADN IPGVIYQLRL NQNGSFSMSY
ISSGCYELYE VTAEELISTG RSIRSFEHPE DVTKIDEAIL NSAQNLTPFQ YQWRIITPSG
QIKWIQALSQ PERQENNELI WDGVILDISQ RQAALQERKR AETERQKKAE ALETALQELQ
QTQIQLVQNE KMSALGNLVA GVAHEINNPI AFLGGNIQPA LEHIQDLFGL VDLYQEKYPH
PEAEIENEII AIDLDYIRED LPNLVGSMRE GVKRICEISN SLRTFSRKDS NCPVACNLHD
GIDSTIMILK HRLKASDSRP EIQIIKQYGE IPSIECFAGQ LNQVFMNLLA NAIDALEESN
IGYTYAQIKA NPNLIIITTQ IADNPRQIII SIKDNGKGMT PEVKQKIFDH LFTTKSVGKG
TGLGLAIARQ IVVEKHHGAI DVNSTLGEGS EFLIRLPF
//
