ID A0A0Q8QRY4_9SPHN Unreviewed; 793 AA.
AC A0A0Q8QRY4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE22_23090 {ECO:0000313|EMBL:KRB88315.1};
OS Sphingomonas sp. Root720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB88315.1, ECO:0000313|Proteomes:UP000051570};
RN [1] {ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB88315.1, ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|EMBL:KRB88315.1,
RC ECO:0000313|Proteomes:UP000051570};
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:KRB88315.1}.
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DR EMBL; LMID01000015; KRB88315.1; -; Genomic_DNA.
DR RefSeq; WP_056365900.1; NZ_LMID01000015.1.
DR AlphaFoldDB; A0A0Q8QRY4; -.
DR STRING; 1736595.ASE22_23090; -.
DR Proteomes; UP000051570; 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; cd00082; HisKA; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 2.
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.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KRB88315.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051570};
KW Transferase {ECO:0000313|EMBL:KRB88315.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 568..787
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 793 AA; 85762 MW; 7C6123AFF423ED17 CRC64;
MSQMIQLDPV AALMLAIIVA LWVAAAVASI IMGLRRDAIA KTRMRDFERQ GALLASAPAV
PFRVGLDGRI GADPRLAHWL GLPAPPATID EMAGDGEGGI SVVDAEGLAA DIAAANQAGR
AFERVLRLAG TDRVVLARGR PAPPAIGDGV IIWLFDNSAA ERTIGRLSAE GQAVSDALDS
CLALIEAAPF PMWHRGPDLK LALVNSAYVA AVEGESAEDV VTRGVELVDS ADGRTPRATA
LAARDGGRIK THVVPVTLGG QRRTMRIVDV PMGEHGVAGY AFDIQDLEQT RGELGRFQEA
QRELFDRLSA GVAQFAPDRS LVFFNQPFLQ FFSLLPEWMT DHPEFDRVLE RMRETQRLPE
ARDFPGWKAD RRAWFNAVDA VEENWTLPGG QHLRVVAQPL PNGGLLLFFE DRTEQVQLSS
ARDTLLRVRT ATFENLFEAI GVFASDGRLH IWNQSFRDIW GLSDADLAQN LRVDAMVELV
AAKLADPSRA QLLRDLVRIA TVDRQARTGR MALADGRYFD FAVVPLPDGN ALFTLLDITA
SRGIEEALRG RADALEEADK LKTAFVANMS YELRVPLTSI AGFAELLDAG YAGTLPTVAG
EYVKAILASV GRLGSLVEDV LDLTQGAAGN LPLAEEHVDM EMLLDDAVAA ARPAAEGKPL
QLVVDIEPGL GAMRGDPRRL RQIADHLLNN AITYTPPQGK VTVRVRGDED MIVWTVADTG
QGMDAAQRAG IFDSYPRIDA SNDEGKQLIG IGLPLTRQLV EAHGGSIALE SEPGRGTTVT
IHLPRHHGEP LHV
//
