ID A0A0S9BY91_9MICC Unreviewed; 569 AA.
AC A0A0S9BY91;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE96_12215 {ECO:0000313|EMBL:KQN86351.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN86351.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN86351.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN86351.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN86351.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN86351.1,
RC ECO:0000313|Proteomes:UP000051467};
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:KQN86351.1}.
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DR EMBL; LMLR01000013; KQN86351.1; -; Genomic_DNA.
DR RefSeq; WP_056431112.1; NZ_LMLR01000013.1.
DR AlphaFoldDB; A0A0S9BY91; -.
DR STRING; 1736232.ASE96_12215; -.
DR OrthoDB; 9792686at2; -.
DR Proteomes; UP000051467; 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; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF17203; sCache_3_2; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQN86351.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..569
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006650752"
FT DOMAIN 209..248
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 337..555
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 247..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 59307 MW; 744E30617F252BC4 CRC64;
MIHRWSIARR LFVAHLLFML ALTAVVGTAT FVDARDQAYD EAGRRMAAVA TTMADNPLVL
DAAGAADPTP LLQPYALKVM ADADADFITI MAPDRTRWTH PKNEELGKPY IGSIDAALNG
QVFTEITAGT LGPSVRTIAP VKDADGTVRA LVAAGVTVRT VDIAVSGRLP ALLAIGLALL
AGGSAASWLL GRYLRQVTRG WGPEQLAQLF AYYESVLHSV REGVILIDPK GKVVMYNDQA
AELLGLAPRT SNPGDAAAGG DGTAADGGRQ EAPSLADLPL APSLRELFES GRTALDEIHL
TGSRILVVNQ GPAVGPGSAA GRTGAAVYGT VATIRDRTEI ESLGSELETM RTLSDALRAQ
THEHANRLHT IVSLMELGRG TEALDFATQD LELSQRLTDD LVSSIEEPVL GALIMGKAAE
AHERGVELTL NTGGNGHGPT PVTGLAVQDL VAILGNLLDN AIDAAAEAPA PRLVELTVEA
SPGALEITVE DSGPGIDPQA VDDIFRHGFS TKSPGPFGRG LGLALVRQAV QRLGGTMTIT
SPAGALFRVT LPTSPAASTA TSLTTEGQQ
//
