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Database: UniProt
Entry: K9XDC6_9CHRO
LinkDB: K9XDC6_9CHRO
Original site: K9XDC6_9CHRO 
ID   K9XDC6_9CHRO            Unreviewed;       834 AA.
AC   K9XDC6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-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=Glo7428_2093 {ECO:0000313|EMBL:AFZ30630.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ30630.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ30630.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ30630.1,
RC   ECO:0000313|Proteomes:UP000010476};
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 chromosome of genome of Gloeocapsa sp. PCC 7428.";
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; CP003646; AFZ30630.1; -; Genomic_DNA.
DR   RefSeq; WP_015188503.1; NC_019745.1.
DR   AlphaFoldDB; K9XDC6; -.
DR   STRING; 1173026.Glo7428_2093; -.
DR   KEGG; glp:Glo7428_2093; -.
DR   PATRIC; fig|1173026.3.peg.2231; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_44_3; -.
DR   OrthoDB; 5555607at2; -.
DR   Proteomes; UP000010476; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd17580; REC_2_DhkD-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ30630.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010476};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          262..314
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          315..385
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          388..440
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          465..683
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          708..824
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         757
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   834 AA;  92992 MW;  1836F443633921C1 CRC64;
     MTQRSPDPTP ITPPIPANEA ERLAALHRYQ ILDTPPEAAF DRITSLAARL FNAPIALVSL
     LDESRAWFKS GYGFEPREVE RNDTICSFAV LSDDVLVALD TQQDPRFSCN PFVQSDPGVR
     CYIGAPLITH DGFNLGTLCL LDTQPREAFS LEQQAMLVDL AAIVVDELEL RLAARQVAQQ
     ELAQRESEAQ LQRALQIGKM GTWDWNLPTN KIIWSAGHFT LLGLQPDQCE PGYEVWLNSL
     HPEDREGAEA ALQRAMTEQT EYRHEYRTVW QDGSIHWVEA RGSFSYNASG QPDRMVGVLV
     DITERKQAEA DLRESEARYR LLAEAIPQFV WITNPDGQNE YVNQQFCDYT GLTPQQMRGL
     DWLSIIHPDD LAMTRDRWLA AVKTGLFYEI EYRFRRADGT YRWFLGQGLP LKDEQGRVLK
     WFGTCTDIEP QKQIERSRLH LLEQEQAARA SAEQANRIKD EFLAVLSHEL RTPLNPILGW
     SRMLRSGNLD AAKTAHALET IERNAKLQTQ LIEDLLDVSR ILQGKFSLNR VPVDVAATIS
     AALETVRLAA EAKSIQIQTN LDTSVGQVVG DTARLQQVVW NLLSNAVKFT PQGGQIEVEL
     KQIGSQAQIT VRDTGKGIVP EFLPHVFEYF RQADGATTRR FGGLGLGLAI VHHLVELHGG
     TVQADSPGEG QGATFTVRLP LMQVATLLRD EAHVPVSMVD DSPLTGIQIL VVDDEADSRE
     FVAFVLEQAG AVVNSVSSGT EALQTITQAT PDLVVSDIGM PEMDGYMLLQ QIRSQESGKQ
     VPAIALTAYA GEYDRQQALQ AGFHQHLSKP IEPNELIESI VNLKRKATRL EPMS
//
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