ID A0A345YJ92_9SPHN Unreviewed; 486 AA.
AC A0A345YJ92;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DVR09_16195 {ECO:0000313|EMBL:AXK43994.1};
OS Erythrobacter aureus.
OG Plasmid unnamed {ECO:0000313|EMBL:AXK43994.1,
OG ECO:0000313|Proteomes:UP000254508}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=2182384 {ECO:0000313|EMBL:AXK43994.1, ECO:0000313|Proteomes:UP000254508};
RN [1] {ECO:0000313|EMBL:AXK43994.1, ECO:0000313|Proteomes:UP000254508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YH-07 {ECO:0000313|EMBL:AXK43994.1,
RC ECO:0000313|Proteomes:UP000254508};
RC PLASMID=unnamed {ECO:0000313|EMBL:AXK43994.1,
RC ECO:0000313|Proteomes:UP000254508};
RA Tang T., Liu Q., Sun X.;
RT "Genome sequence of Erythrobacter strain YH-07, an antagonistic bacterium
RT isolated from Yellow Sea.";
RL Submitted (JUL-2018) 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};
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DR EMBL; CP031358; AXK43994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345YJ92; -.
DR KEGG; err:DVR09_16195; -.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000254508; Plasmid unnamed.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.250.2580; -; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:AXK43994.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254508}.
FT DOMAIN 6..76
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 271..485
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 486 AA; 54291 MW; DFB8D5B084741469 CRC64;
MLYGVTDEQV SSLLQNWKVG VVGLRPDFTL EFVNAEAERI DGRVAEELIG RSVWEVLPNV
VGTEVEELIR LAMETRKGGT APLYRTSRPG RTIFLEIRVQ PWGKGVALFI LDVTNWVQLE
SEKERLEEKY MLASRASPDI QYEWNIKDNI WDSQGGHESL YPGIVTPTEI GEFTARIHPD
DRERMNTLFR QTLLSGKAHW AFEYRVNRNG VWANVEDRAF IVYDEEGMPV RAVGVMKDVS
ETAARQMEIT RLQSELIHVS RVSAMGTMAS VLAHELNQPL AAIGSYLAGA ERLLEEADEI
DRELLLQAVR EAHAGSSRAG KIIQRLRSMT MKAEHKRDWT NISKAVDNAV SLALIGRTEL
RDTLSIDISP KLQVQADEIQ IEQVLLNLIR NALEANEEAG RSGVKISARE LSVDMIGISI
ADVGNGIPAD LQPKLFDFFV STKDDGMGIG LPISRTIVEA HGGKISIEDR EPYGAVFRLM
LPINGH
//