ID G2NRP3_STREK Unreviewed; 395 AA.
AC G2NRP3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SACTE_6197 {ECO:0000313|EMBL:AEN13972.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN13972.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN13972.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN13972.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002993; AEN13972.1; -; Genomic_DNA.
DR RefSeq; WP_014049921.1; NC_015953.1.
DR AlphaFoldDB; G2NRP3; -.
DR STRING; 862751.SACTE_6197; -.
DR KEGG; ssx:SACTE_6197; -.
DR PATRIC; fig|862751.12.peg.6432; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_0_11; -.
DR OrthoDB; 2514702at2; -.
DR Proteomes; UP000001397; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AEN13972.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW Transferase {ECO:0000313|EMBL:AEN13972.1}.
FT DOMAIN 288..389
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 395 AA; 42923 MW; 7A113036B8DF0AD4 CRC64;
MTGAGVAVVT VLAALLLGTG FLLGRAARPQ RTSDVGTPVE HATFETLHTA SLAAPPLRAG
LTEESARRSA RRLRSLLGTD ALCLTDRDRV LVWDGEGDHH GREVMDHVRG LLDSGRDTAF
RTDCGDLDCP LRWAVAVPLT VDHRVLGTLV AWAPRESAVL ARAAGEVARW VCVQLELAEL
DRSRTQLIEA EIKALRAQIS PHFIFNSLAA IASFVRTDPE RARELLLEFA DFTRYSFRRH
GEFTTLADEL HSIDQYLALV RARFGARLSV TLQVAPEVLP VALPFLCLQP LVENAVKHGL
EGAVRTSRIT ISALDAGAEA EVVIEDDGIG MEPERLRKIL RGEGGTSTGI GLLNVDERLR
QVYGDAYGLV IETGVGAGMR ITLRLPKYRA GVHGS
//