ID A0A0S9Q996_9ACTN Unreviewed; 722 AA.
AC A0A0S9Q996;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF47_01385 {ECO:0000313|EMBL:KQP66477.1};
OS Nocardioides sp. Leaf285.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP66477.1, ECO:0000313|Proteomes:UP000051495};
RN [1] {ECO:0000313|EMBL:KQP66477.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP66477.1,
RC ECO:0000313|Proteomes:UP000051495};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP66477.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP66477.1,
RC ECO:0000313|Proteomes:UP000051495};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KQP66477.1}.
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DR EMBL; LMNH01000001; KQP66477.1; -; Genomic_DNA.
DR RefSeq; WP_056862234.1; NZ_LMNH01000001.1.
DR AlphaFoldDB; A0A0S9Q996; -.
DR Proteomes; UP000051495; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR007895; MASE1.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051495};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 315..360
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 398..449
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 474..693
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 722 AA; 74521 MW; 8415402008906F28 CRC64;
MSTTSARRSR ARLAPAGPVT HGTPRRVLLL LAVLLGALAG MQTVAAGSLT PTVWPPAGLA
AGLYLTTPPR RRPHVVGALL GLLVLAHLLD GAGGRVSLGL AVSTVLGAVV TETLLVARRP
DGRARLRDQG DVSRMIGAIA VGSAVAGAGW VATLLLTGGP VESTWRVALA AAGAHAAAAV
VLVPLFLDKL EFQALASTGE RAVQLALTVG TTVAVFVPTD LPQLIFAVMP MFTWHAFRGS
LRESMVVLVV VAVVSTTLTT AGLGPVAAAG ALLDLPPEVS LGVLQLFLLD CGLILLPLSV
MVTQQRVATA CAEQERETMI RLVDAATGTA VVATAADGTV TLFNPGAAAV FGRRADEVVG
CRPDALFTEA ELRRHADAVG AAPVFADICR ASVAQGVRDA HWRVRRGEEE RILRMTLTAV
PDSVGGLTGY LATAEDVTDR ERAHRSLLAT LEAEREAVER LSSLERTKTE LVATVSHELR
TPITSILGFA EVLEDGDVGE LTGPQRAVLT RISSNSRRLS ALVEDLLMLS SVEEATVRLQ
VESLDLRDVV ARAAAAVVDC VPERSLDVAL HLPPGPVVLG GDAGKLERAV TNLVSNALKF
TPDGGAVTVA VEPGADEHVV VVSDTGIGIA QEEQAHLFTR FFRSAEANLR AIQGTGLGLS
IVQAIVELHG GRVGVDSAPG VGTTVTVVLP LVMPSVLSSA VPLGAPASGP AGGGEGLAVL
PA
//
