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Database: UniProt
Entry: K9WJT6_9CYAN
LinkDB: K9WJT6_9CYAN
Original site: K9WJT6_9CYAN 
ID   K9WJT6_9CYAN            Unreviewed;      2077 AA.
AC   K9WJT6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Mic7113_4337 {ECO:0000313|EMBL:AFZ20034.1};
OS   Allocoleopsis franciscana PCC 7113.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ20034.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ20034.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ20034.1,
RC   ECO:0000313|Proteomes:UP000010471};
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., 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 Microcoleus sp. PCC 7113.";
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};
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DR   EMBL; CP003630; AFZ20034.1; -; Genomic_DNA.
DR   RefSeq; WP_015184170.1; NC_019738.1.
DR   STRING; 1173027.Mic7113_4337; -.
DR   KEGG; mic:Mic7113_4337; -.
DR   PATRIC; fig|1173027.3.peg.4792; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_34_2_3; -.
DR   OrthoDB; 517727at2; -.
DR   Proteomes; UP000010471; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 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; IPR013656; PAS_4.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
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; PF08448; PAS_4; 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   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   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010471}.
FT   DOMAIN          7..288
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1608..1644
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1687..1739
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1791..2072
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          348..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1752..1782
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2077 AA;  231795 MW;  7EA2A3346F7AFA13 CRC64;
     MLLLNNITVK ATIYESANSL VYRGIKNYDN TPVILKVLKE DYPSPQEIVR YKKEYAITHS
     LNLEGVIKAY SQQEYQRSLV IVLEDFGGES LKKWMKLSPQ GYYPMPLPEF LSLAIKITKI
     LGNIHSSNVI HKDINPGNIV LNPETGQVKI IDFGISTRLP SNSPPLVHPH GLEGTLAYMS
     PEQTGRMNRT LDYRTDFYSL GVTFYELLTG KLPFTTDDVL ELVHCHIAKQ PVPPKEGRRQ
     TGALVRTGGR REEVPQSVSD IVIKLLAKNA EDRYQSAWGI QADLEECLRQ VKATGRVENF
     RLGSQDISNK FQIPQKLYGR EAEIETLLAA FKRVAGGELT SPPIPLLPEE GSPTSPFHKE
     KVSSSVLPPR RMDRGGLEGR GGLGCVEMML VAGYSGIGKS ALVQEIYKPI TEKRGYFISG
     KFDQLQRNIP YSAVVHAFGG LMRQLLSESE AQLRQWQEKI LAALGPNAQV IIDVIPEVEL
     IIGKQPPVPE LGGAESQNRF NLVFQNFIRV FCTKEYPLVI FLDDLQWVDS ATLKLIELMM
     TDIDTQYLLL IGAYRDNEVN STHPLMMVLD ELRRQEATIN QITLAPLKLE HISHLIADTL
     HSDTDSVKPL AELVKGKTEG NPFFVNEFLK TLYAENLLVF TPPTPLVNGG VREDSLFKGE
     EREHSLTSGG VQEKLINSPS YQGGVRGGRS LWQWDIAQIE AQNITDNVVE LTIAKLKKLP
     QSTQEVLRLA ACIGANFDLN TLSIICQKSE AVIFQDLLIA IESGLILPVS EFNTELLIQD
     YRFLHDRVQQ AAYALIDESQ KQVVHLQIGR NLLEKTSPEQ RSERLFEIID HLNQGLELVT
     ARSERTEIAR LNLMAGQKAK AATAYDAAFK YFTTGIQRLN SESWQSEYDL TLALYSEAAE
     AAYLQGCFDE MEQLIEVVLV HAKTVVDKVQ VYDSSIQRYL SQGNLKEALK TGLEALKLLG
     IDLIENPSQA DTQRELESTA ALLAEREIED LINLPEIAAP EPLAAITILS NMGSAAFITL
     PALWILIICK TVNLSITYGN TIWSPMYYAA YGFVLCGVVQ DIELGYKFGQ LAITSAERLN
     NKRGKARTLR FSGTHIMQWK VHLSNTIPML ADAYQSGVET GDFECAGYAA YNLCYNSFSA
     GEELTQLEQK TATYSKATNQ IRRESPSNWL AIVWQTILNL LDRSENPSRL VGRVCNEEEA
     LSHAIAVKDG TVIQILYLHK VMLCYLFEEH HQAVQTAILA RKHFEQVSAI MILPVFCFYY
     SLALLSLSLD ASNSEKAAWL NCVNTNQEKM QKWAEHAPMN YLHKFYLVKA EKARVLGQFL
     EAEEFYERAI DGAKENGYLQ EEALAYELAA KFYLERGRLR FARTYMKEAH YTYTIWGAKA
     KVNDLEAKYP QLLTKSSTAK SITSTRTTHP TTTTGSQSGE TLDLATVMKA SQAISGEIVL
     DKLLSSLMKI LIENTGAQTG FLLLEKAGQW VIEASGTVNS DNVPVFQSLS IDNHLPTSII
     NYVVRMKEIV VFNDAASEIQ NPPPNSPLGK GGTKIPNLND PYIKAHQTKS LLCTPLINQG
     QLRGIVYLEN NLTIGAFTPE RLEILQLLSG QAAIAITNAK LYAEVHASER RLTQFLEAIP
     VGIGVLDASG KPYYANRTAI ELLGKGVVPS ATAEQLGEVY QVYIAGTDQQ YPSEQMSIVR
     ALRGECATID DVEIHHPDRV IPIESRGTPI FDEKGNVAYA IGAFQDITDR KQAQKLLTDY
     NHILEAQVAE RTEALHQQAQ ELKLTLERLQ RTQSQLIQAE KMSSLGQMVA GIAHEINNPT
     SFIYGNISPA TGYAQDLLHL IALYQQYYPE PVAEIAAQID AIEPNFIAED FPKLLASIRQ
     GAERIMQIVL SLRNFSRLDE RECKRVDIHQ GIDNTLVILQ HRLKQQPNRP EIQVIKEYSE
     LPNVECYAAQ LNQVFMNILN NAIDALENVR SSSYSLAQEA SYIVHSKVAE LGRSNEQSTM
     NYEQSPTIWI STEVVEQNRV VIRIANNGSA IDPALHSKIF DPFFTTKPVG SGTGLGLSIS
     YQIVVERHGG ELTCHSTPEQ ITEFAIALPI TQGKKSM
//
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