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Database: UniProt
Entry: K8GGX6_9CYAN
LinkDB: K8GGX6_9CYAN
Original site: K8GGX6_9CYAN 
ID   K8GGX6_9CYAN            Unreviewed;      1076 AA.
AC   K8GGX6;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=OsccyDRAFT_4860 {ECO:0000313|EMBL:EKQ67039.1};
OS   Leptolyngbyaceae cyanobacterium JSC-12.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX   NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ67039.1, ECO:0000313|Proteomes:UP000001332};
RN   [1] {ECO:0000313|EMBL:EKQ67039.1, ECO:0000313|Proteomes:UP000001332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ67039.1,
RC   ECO:0000313|Proteomes:UP000001332};
RG   DOE Joint Genome Institute;
RA   Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT   "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL   Submitted (OCT-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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKQ67039.1}.
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DR   EMBL; AJUB01000019; EKQ67039.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8GGX6; -.
DR   STRING; 864702.OsccyDRAFT_4860; -.
DR   PATRIC; fig|864702.5.peg.5243; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_114_10_3; -.
DR   OrthoDB; 567946at2; -.
DR   Proteomes; UP000001332; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; IPR003660; HAMP_dom.
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; 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   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43047:SF72; PHOSPHOTRANSFERASE RCSD; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 4.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 3.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001332};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        229..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          248..301
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          310..357
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          384..434
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          435..507
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          511..563
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          691..761
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          765..817
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          821..1072
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          674..701
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1076 AA;  121466 MW;  CDDEB2936294B2F1 CRC64;
     MPSSRSLPRS SPKIPLHWVL VIPFVLQTVG AVGIVGWLSY RSGQKVVEQI AYQLLETVSE
     QVSDRLDTLL QAQQQEIATN PQTAAQGNLS PQKLQSLRTR LNPYLSHLDF SPSSFVFIVE
     PSGNLVATST LNNSLLPGGR YQPKRFASAN GQDARIHKIS QQLLDSFGSF RNFQQTTQLT
     LKTSQTGEQP QFVQVTPYQG KGRLDWLIIT VVPESDFIGE IQTNLWRTVL LSFLTLMCTT
     ATGVLTAFWI AKPIRQLSRA SQTLASGQWQ QSLQEDSWIT ELSVLAKSFN RTADQLQQSF
     DRIKVALQAS EEKFTKVFRT SPDPITIMTL DEGRYLEVNE SFLKFSEYSQ EEVIGRTSAE
     LNLSVDYQQD LALKEQLERQ GTVQNFEYYY RTKTGQVGTT LLSIERVELD GQQRILTIAK
     DISDRKQTEH ALRQAIQQIN TYFEHSPLAI MEWDQTGRIL RWSTQAERVF GWTADEIQER
     RWQEWEIVHE DDQDRVITEL TPLMNGLTTS HMLQNRNRTK DGRVIVCEWY SSAIFDETGN
     LISVLSFAQD ITERIQMETA LQESEARNRA ILQAIPDLMI LYTAEGTYVD IIQRNLAQDA
     ITDPDPVGKH ISELLPSDIA ERQINASKQV LATGEIVVYE QELWIQGTLQ YEEVRVVPCG
     EETVLVIVRD ISDRKRNEIE RQLAEEALQH SEEQIRRAFE DAAIGMAIVG LDGRFLRVSH
     SLCEIVGYSE TELLAMTFHE ITHPDDLLTD LGYSEQMLSG ELRTYQLEKR YIHKQGYIIW
     ILVNVSLVKD NNDQPLYFVS QIQDISDRHE LDRIKNEFIS IVSHELRTPL TAIRGSLGIL
     ATGVLAHEPD TAKAMLHVAL NNSERLVRLV NDILDLERLE SGKTQLVMEE CSVNNLLMQA
     IESVQTLVAQ ASISLKVTSC AAKVWASPDA IVQTLTNLIG NAVKFSEPGS TVWLKAELKN
     GEWEMGEEAA IEIWESQRPA VSSSTSLSSS PYSQPFILFS VADQGRGIPP EKLESIFGRF
     QQVDVSDSRD KCGTGLGLAI CKSIVQQHGG KIWVTSVLNE GSTFYFTVPQ ANRKEE
//
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