ID A0A0Q9T5B3_9ACTN Unreviewed; 463 AA.
AC A0A0Q9T5B3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG94_11300 {ECO:0000313|EMBL:KRF34749.1};
OS Nocardioides sp. Soil805.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736416 {ECO:0000313|EMBL:KRF34749.1, ECO:0000313|Proteomes:UP000051356};
RN [1] {ECO:0000313|EMBL:KRF34749.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF34749.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF34749.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF34749.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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};
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:KRF34749.1}.
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DR EMBL; LMSU01000002; KRF34749.1; -; Genomic_DNA.
DR RefSeq; WP_056926572.1; NZ_LMSU01000002.1.
DR AlphaFoldDB; A0A0Q9T5B3; -.
DR STRING; 1736416.ASG94_11300; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000051356; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
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 InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
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; SSF158472; HAMP domain-like; 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:KRF34749.1};
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 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..242
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 250..459
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 443..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 49531 MW; B3374CDDC23C96CE CRC64;
MSSLAGWDDK RWHYRRSLAS RVAVLTTLAV AVSIAAMSLG AFMVMRMQLQ GSLDESLLDR
AEKAAKYTAL SQMTERKVPS WMLGAADVRI AFITAGGAVV TADEGPQIVL GTPEHDVAVG
RRQESVRTIV TAGGVEYRVA TVPAGPDQAL VLAQLLSSQQ RTLAKLGTVM LVAGGLGVLA
AALAGWAVAA NGLRPVRRLT RSVERIAVTE DLAPLAVEGD DEIARLAGAF NQMLTSLAAS
RDRQRRLVAD AGHELRTPLT SLRTNLDLLA QADTDGGLPE EARRELLDDV RAQIEELTTL
VGDLVVLARE DHPAAIIEPV DLAEVTERAL VRVRRRAPGV DFDVRLDHWR VTGDATGLER
AILNLLDNAA KWSPIGGTIT VRLMSGVLTI DDQGPGIPAE DQARVFERFW RSDESRSMPG
SGLGLAIVRQ VVDRHGGRVA VDDAPGGGTR LTLSLPGEQP AHA
//
