ID A0A0Q7ZL79_9ACTN Unreviewed; 465 AA.
AC A0A0Q7ZL79;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASD66_14555 {ECO:0000313|EMBL:KQZ70785.1};
OS Nocardioides sp. Root151.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ70785.1, ECO:0000313|Proteomes:UP000051274};
RN [1] {ECO:0000313|EMBL:KQZ70785.1, ECO:0000313|Proteomes:UP000051274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ70785.1,
RC ECO:0000313|Proteomes:UP000051274};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ70785.1, ECO:0000313|Proteomes:UP000051274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ70785.1,
RC ECO:0000313|Proteomes:UP000051274};
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:KQZ70785.1}.
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DR EMBL; LMGG01000004; KQZ70785.1; -; Genomic_DNA.
DR RefSeq; WP_056891383.1; NZ_LMGG01000004.1.
DR AlphaFoldDB; A0A0Q7ZL79; -.
DR Proteomes; UP000051274; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQZ70785.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051274};
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 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 180..234
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 242..433
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 268..295
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 465 AA; 49840 MW; 099E1953140CD593 CRC64;
MRRLPLRVRL VAGFSAAMFV VLLAAGAFVY SRVHYALDRG LDSDLARATE TLTPLVGPTG
TMTNRASAEA TGVAWQVLGA DGTVLDHGGP AGSSAMVSTR VLREVDSNPS TVDVGDLLPA
SKDPYRVQIV KVSGTPTRYV LVGVRRDHRD EALRELLLQL ALAGFGALLV TGFVGERLAR
AALRPVERYR RQAADIAAGA TDLRLQVPAT RDDEVTRLGH TFNDMLASLE RSLDRERQFV
NEASHELRTP VTLIGSRIQL ARRRSRSVTE HERILDELQV DVDRLADLAE DLLQLGSAGA
RTGTGDLATI AARVVDQRRV VDPRHAVEVS LSSLVSTLRV ALDELAIERI LTNLLDNASA
HGAPPHDVRL DHPDPSWARL QVTDGGDGMP PDLLATATRR FTRAGEARSR PGAGLGLALV
ASLTVSCGGE LRLCFDGHHV SHGLSVPVPC VHGPAMTATV LLPTA
//
