ID A0A0Q6VLN8_9BURK Unreviewed; 651 AA.
AC A0A0Q6VLN8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASD15_18890 {ECO:0000313|EMBL:KQV79397.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV79397.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV79397.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV79397.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV79397.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV79397.1,
RC ECO:0000313|Proteomes:UP000051876};
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:KQV79397.1}.
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DR EMBL; LMDJ01000034; KQV79397.1; -; Genomic_DNA.
DR RefSeq; WP_057158207.1; NZ_LMDJ01000034.1.
DR AlphaFoldDB; A0A0Q6VLN8; -.
DR OrthoDB; 9812260at2; -.
DR Proteomes; UP000051876; Unassembled WGS sequence.
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; 3.30.450.40; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KQV79397.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051876};
KW Transferase {ECO:0000313|EMBL:KQV79397.1}.
FT DOMAIN 414..645
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 371..398
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 651 AA; 71979 MW; 7A24C96B96E01396 CRC64;
MESRLSRLEA VQSILLEIGQ KSSTCTDIAE FVQAVHEALG RIMYTANFYV ALSDEGRPNS
VRFVYFVDEV DEAPDRSEVV ELASPEQSPT AWVILNRQRL IMTAEEHNSR GVDGSTWGLG
TTAEHWMGCP LVDHNHQVLG AMVIQSYDKQ HTFNEEDQAL FQLIANHVSG ALQGLQSMDR
LERAVHERTA ALEYEVAERR RAENLQRALY EIASLSGGAW DRATMYQRLH QAISEVLTVR
NFLIALYHPS NNEITVPYFV DEKDPTAPCT SFSYGVGMTS YILKQRQPVL LDREGYLALM
ASGDVERPLG NEDIVSWMGA PILLNDYAYG VLVVQSYDED MIYSQSDLDV LAFMASHVAV
VISRLQADRA IRRAKTALEE QNAALNTALT QLQTAQGELV RQEKLASLGR LVAGVAHEIN
TPLGICVTAT SHLVQELKLT KEDLASGALD EEGLNQFFDI VDQTLRIMTT NTQRAAALVR
SFKQVAVDQS SDNVRSFNLR KYLDEVLLSL QPKLKGKPIE VQVDCPPDIQ MESFPGAVSQ
IVTNMVVNSL VHGFGDGQSG SIKIKGRIEG EHVHFDYSDD GIGMDQGTLS QLFDPFFTTK
RGSGGSGLGA HILYNLVTGP LGGTIKVVSA PNMGLHYNLR FPRVQHGKPQ V
//