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Database: UniProt
Entry: I0R3F7_9MICO
LinkDB: I0R3F7_9MICO
Original site: I0R3F7_9MICO 
ID   I0R3F7_9MICO            Unreviewed;       353 AA.
AC   I0R3F7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Sensor-like histidine kinase SenX3 {ECO:0000256|ARBA:ARBA00039401};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=IMCC13023_01340 {ECO:0000313|EMBL:EIC92393.1};
OS   Candidatus Aquiluna sp. IMCC13023.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Aquiluna.
OX   NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC92393.1, ECO:0000313|Proteomes:UP000054510};
RN   [1] {ECO:0000313|Proteomes:UP000054510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX   PubMed=22689238; DOI=10.1128/JB.00586-12;
RA   Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT   "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT   member of the Actinobacteria isolated from an arctic fjord.";
RL   J. Bacteriol. 194:3550-3551(2012).
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:EIC92393.1}.
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DR   EMBL; AJKR01000001; EIC92393.1; -; Genomic_DNA.
DR   RefSeq; WP_007540182.1; NZ_AJKR01000001.1.
DR   AlphaFoldDB; I0R3F7; -.
DR   STRING; 1081644.IMCC13023_01340; -.
DR   PATRIC; fig|1081644.3.peg.137; -.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000054510; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EIC92393.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054510};
KW   Transferase {ECO:0000313|EMBL:EIC92393.1}.
FT   DOMAIN          133..349
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   353 AA;  38298 MW;  61DEFA6A77681822 CRC64;
     MGILSNKKAN QADARQVDAF EIVAAQVVDV LATAGVVLDE RNLVLRASPG AIQFGLVQNR
     HLIHSALVRL VEDARSTSGA AEQELQIEAG LQREQLWVHA RAAKFGDRYV MLLVDDRTEA
     KRLEVTRRDF VANVSHELKT PIGAISLLTE AIAGAHDDPD TIRKFSASLQ KEAARLGSLV
     QELMQLSRVQ GANLSDTAVE LDLALVINDA VDRNQVLAEQ RGVKLVTSAI KGSRMVGDYE
     MLTTAVRNLV ENAIAYSDKG SQVGIGLKEI GGVAEIAVTD SGIGISEDEQ ERIFERFYRV
     DPSRSRDTGG TGLGLSIVKH AASNHKGEVR LFSKEGVGST FTLRLPIQNR ETN
//
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