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Database: UniProt
Entry: U5QG84_9CYAN
LinkDB: U5QG84_9CYAN
Original site: U5QG84_9CYAN 
ID   U5QG84_9CYAN            Unreviewed;       601 AA.
AC   U5QG84;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   10-APR-2019, entry version 36.
DE   SubName: Full=Multi-sensor signal transduction histidine kinase {ECO:0000313|EMBL:AGY56685.1};
GN   ORFNames=GKIL_0439 {ECO:0000313|EMBL:AGY56685.1};
OS   Gloeobacter kilaueensis JS1.
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales;
OC   Gloeobacteraceae; Gloeobacter.
OX   NCBI_TaxID=1183438 {ECO:0000313|EMBL:AGY56685.1, ECO:0000313|Proteomes:UP000017396};
RN   [1] {ECO:0000313|EMBL:AGY56685.1, ECO:0000313|Proteomes:UP000017396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS {ECO:0000313|Proteomes:UP000017396};
RX   PubMed=24194836; DOI=10.1371/journal.pone.0076376;
RA   Saw J.H., Schatz M., Brown M.V., Kunkel D.D., Foster J.S., Shick H.,
RA   Christensen S., Hou S., Wan X., Donachie S.P.;
RT   "Cultivation and Complete Genome Sequencing of Gloeobacter kilaueensis
RT   sp. nov., from a Lava Cave in Kilauea Caldera, Hawai'i.";
RL   PLoS ONE 8:E76376-E76376(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC         Evidence={ECO:0000256|SAAS:SAAS01118672};
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DR   EMBL; CP003587; AGY56685.1; -; Genomic_DNA.
DR   RefSeq; WP_023171708.1; NC_022600.1.
DR   STRING; 1183438.GKIL_0439; -.
DR   EnsemblBacteria; AGY56685; AGY56685; GKIL_0439.
DR   KEGG; glj:GKIL_0439; -.
DR   PATRIC; fig|1183438.3.peg.439; -.
DR   OrthoDB; 1755994at2; -.
DR   BioCyc; GKIL1183438:G1HLA-424-MONOMER; -.
DR   Proteomes; UP000017396; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR007891; CHASE3.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017396};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914, ECO:0000313|EMBL:AGY56685.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017396};
KW   Transferase {ECO:0000256|SAAS:SAAS01003669};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    185    207       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      231    273       PAS. {ECO:0000259|PROSITE:PS50112}.
FT   DOMAIN      306    356       PAC. {ECO:0000259|PROSITE:PS50113}.
FT   DOMAIN      385    601       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   COILED      207    227       {ECO:0000256|SAM:Coils}.
FT   COILED      347    382       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   601 AA;  67572 MW;  6F0B22C2DD12E5E8 CRC64;
     MQRFLLDERS FRRSLLWSVL LPLLLVAVLA GVLLWQVGAL LEANRWVEHT SNVIGALNRT
     ERLLVDGETG LRGYLLTGER RFLEPHERSR TTLGGQFSTL ASLVVDNREQ SERVNRLRTR
     AESWQLYARG RLTASGAQRA NLQANLEGKR RMDELRTLIQ QMLSVEENLR AIRTSTAQST
     ASGTILLALV ALGTAGVILV VFVRARLVQL DDEYRKLLKQ TRSQTEELAK REERFRRVVE
     SNIVGILFAD LEGQIHEAND AFLQTVGYSR EELARGQLRW DRITPGEYTP ADARAVAQLR
     QSGRCEVFEK AYVRKDGAQV QVLVGAALLP DSDSDEAVSF VVDVSERVRA EVQLRQLAET
     LEEKVEARTD QLQQANRELE QYAFVVAHDL RAPLRSIQGF VEAIVEDCGR TLNGECREYL
     ERIDFSGRRM EQLIDDLLAY SRLGSTEIET RAISLEAAVS RALEELSADI QRSSAVIRVE
     RPLPAVQADR VILVQVLTNL LSNAIKFVAP SVTPRVRVYA RQNTSQARVR LWVEDNGIGI
     APDRQERIWG VFERLHGFET YPGTGIGLAI VQRGCERMGG RAGVESQKDS GSRFFIDLAE
     G
//
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