ID A0A0T0PX61_9SPHN Unreviewed; 784 AA.
AC A0A0T0PX61;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG29_06380 {ECO:0000313|EMBL:KQT33634.1};
OS Sphingomonas sp. Leaf412.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT33634.1, ECO:0000313|Proteomes:UP000051178};
RN [1] {ECO:0000313|EMBL:KQT33634.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT33634.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT33634.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT33634.1,
RC ECO:0000313|Proteomes:UP000051178};
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:KQT33634.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMQP01000002; KQT33634.1; -; Genomic_DNA.
DR RefSeq; WP_055981823.1; NZ_LMQP01000002.1.
DR AlphaFoldDB; A0A0T0PX61; -.
DR STRING; 1736370.ASG29_06380; -.
DR OrthoDB; 9797304at2; -.
DR Proteomes; UP000051178; 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; cd00075; HATPase; 1.
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; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KQT33634.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051178};
KW Transferase {ECO:0000313|EMBL:KQT33634.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 560..781
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 784 AA; 85438 MW; B6054B304C2FC43E CRC64;
MIAIDGLTAI GAGVLVALIV AGAVAMLAIG LRARRAAAGD ARQRARLEAL LDTAPMQPVV
VRPDGRVEMP RRVADWLGLD APADYLDRLA GDDGWGLDAI DATALNADVQ ACLRAARGFL
RTVHCDGGQR ALTVQGERRG DAVVLWVFDS TATEGEVRLL TAEIADLSQA FDALTGLVEA
APLPIWYRDS DLNLAMVNSA YVAAVEGTDA ADVVARGVEL VEGMTQAQAG AVAARESGRA
QQRILPATID GARRALRLHD VPLPVGGFAG FAVDVEELEQ ANARERRFAE AQRATLDRLS
AGVAQFGPDR ALAFFNQPFR RMFAMRREWL SDRPEFDRVL ERMREAKRVP EVRDFPGWKA
ERRGWFLQTD GALEEAWHLP GGTHLRVVAQ PLPDGGLLLV FEDRTEQVQL ASARDTLLRV
RTATFDNLFE ALGVFAADGR LQLWNNRFRA LWDFEEEFLS SHPRVDAIAE RVATRLANPQ
HARFISELVR YATQERKQRA GQVALSDGRH FEFAAVPLPD GNALFTMLDI SDSRRMEQAL
RDRNEALEAA DRVKTAFVAN MSYELRTPLT SISGFAEMLH AGFAGTLSPE ATGYVGAILD
SAERLGLLID DVLDLTTTAD SETLERADVD VAVVARTAAD ALRPSAKRHA VDYVIDVQHS
VGRLNADARR IREIVEHLLR HAIASASAGD RQGGSVLLRA DGNARMARIL VSDDGEGMDA
EMQANAFDRF AETQMAPGTD RALGLGLPLA KQFVEAHGGT IKLQSERGKG TLVTVELPRR
ADGR
//
