ID A0A0Q9SQR3_9MICO Unreviewed; 440 AA.
AC A0A0Q9SQR3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG91_03265 {ECO:0000313|EMBL:KRF30008.1};
OS Phycicoccus sp. Soil802.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736414 {ECO:0000313|EMBL:KRF30008.1, ECO:0000313|Proteomes:UP000050906};
RN [1] {ECO:0000313|EMBL:KRF30008.1, ECO:0000313|Proteomes:UP000050906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF30008.1,
RC ECO:0000313|Proteomes:UP000050906};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF30008.1, ECO:0000313|Proteomes:UP000050906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF30008.1,
RC ECO:0000313|Proteomes:UP000050906};
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:KRF30008.1}.
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DR EMBL; LMSS01000001; KRF30008.1; -; Genomic_DNA.
DR RefSeq; WP_056921133.1; NZ_LMSS01000001.1.
DR AlphaFoldDB; A0A0Q9SQR3; -.
DR Proteomes; UP000050906; 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}; 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 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..224
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 232..439
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 440 AA; 46740 MW; 914184DB24A04A3C CRC64;
MTLGFGLLAL GLSALLSGLA WTLVTRTMVS QTEQTALVET SLDRGEVETA LSTGVADLPT
VLEGVPGTDS AAVLAHVDGR WYATSPSLGP ASLPTSLVTL VGGGQEATQR IRVDGTLHLA
VGLPLDGGRG SYFEIYSLDE MQRTARALSL GLVAAAVVTV LIGLGVGRFA SRLALRPLTE
LNRVAADVAA GQLSARLDAD GDPDLEELAG SFNRTVEDLQ RHVVADARFA VDVSHELRTP
MTTMLNSMQV IQNRREQLPE SVREPVDLLA DELERFRALV VDLLEISRHD AGDQVVRETV
RVGDLVRRAA DAAAGRVVTT VDPAVATLTM EVDKRRLERV VANLVGNAET HGGGCTAVRV
EPGAHRLRIV VEDAGPGIVP ERRARVFERF ARGGSSERTG VGLGLSIVQR HVALHEGQVL
VEERPGGGAR FVVELPTISS
//
