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Database: UniProt
Entry: A0A0G3AL83_9ACTN
LinkDB: A0A0G3AL83_9ACTN
Original site: A0A0G3AL83_9ACTN 
ID   A0A0G3AL83_9ACTN        Unreviewed;       452 AA.
AC   A0A0G3AL83;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ABB07_16935 {ECO:0000313|EMBL:AKJ11659.1};
OS   Streptomyces incarnatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ11659.1, ECO:0000313|Proteomes:UP000035366};
RN   [1] {ECO:0000313|EMBL:AKJ11659.1, ECO:0000313|Proteomes:UP000035366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX   PubMed=26159526;
RA   Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA   Tamura T.;
RT   "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT   the Nucleoside Antibiotic Sinefungin.";
RL   Genome Announc. 3:e00715-e00715(2015).
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; CP011497; AKJ11659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3AL83; -.
DR   STRING; 665007.ABB07_16935; -.
DR   PATRIC; fig|665007.5.peg.3627; -.
DR   Proteomes; UP000035366; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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   NCBIfam; NF041732; hist_kin_CseC; 1.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   SMART; SM00304; HAMP; 1.
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; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AKJ11659.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          168..224
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          232..434
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   452 AA;  48474 MW;  149EE80CD39D21AF CRC64;
     MRGILRHSVR RMERAGLHTG LRWKLSAAIA LVAGLVAITL SLVVHNAARV SMLDNARDLA
     NQRLQWAQRN YETSRRPNFP NVKVDDPELP AALRQKMVDG RKASDVIDHG GVPDIWAALP
     TKDGHVLSTH GPLPDRSTAV MKDLDQALVI GSVAVVFGGS ALGVLIGGQL SGRLRKAAAA
     ANQVAKGETD VRVREAIGGV VRDETDDLAR AVDAMADALQ QRLEAERRVT ADIAHELRTP
     VTGLLTAAEL LPPGRPTELV LDRAKAMRTL VEDVLEVARL DGASERAELQ DIMLGEFVSR
     RVAAKDPEIE VRVVHESEVT TDPRRLERVL FNLLANAARH GRPPIEVTVE GRVIRVRDHG
     PGFPEELLAE GPSRFRTGSK DRAGTGHGLG LTIAAGQARV LGARLTFRNV RPAGTQAGTP
     AEGAVAVLWL PEHAPTATGS HPMMPLSGGS TP
//
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