ID A0A0Q6WV82_9BURK Unreviewed; 605 AA.
AC A0A0Q6WV82;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:KQV91271.1};
GN ORFNames=ASD15_04315 {ECO:0000313|EMBL:KQV91271.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV91271.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV91271.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV91271.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV91271.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV91271.1,
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 -!- 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:KQV91271.1}.
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DR EMBL; LMDJ01000001; KQV91271.1; -; Genomic_DNA.
DR RefSeq; WP_057153470.1; NZ_LMDJ01000001.1.
DR AlphaFoldDB; A0A0Q6WV82; -.
DR OrthoDB; 9806477at2; -.
DR Proteomes; UP000051876; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KQV91271.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051876};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transferase {ECO:0000313|EMBL:KQV91271.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..548
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 605 AA; 64464 MW; 51D9B2360A50AE7B CRC64;
MLNNMTVRAK LITLISVSLL ALLIVMLIGI RGMQHGGEML DDVGRNKLPS VLNLQVVNEG
QTALRSASRA IDALAAYPEQ FAEIERNLRS KHEFWSRIDK AWKIYERLPQ DSDEAALWQQ
FSKEWELWKA ADQRFDQVAG DLLRASGAEQ RKAGFVTLHQ DLIALRPLYS NAENALTKLI
ELNERRATEA VAAAEAQSRN ALLLMYGTAA VALLALSAMG WLVLRGILRQ LGGEPAYAAS
VVHEVAQGNF AVDVRLAAGD NSSLLHSMKQ MVDKLLAQIG GEPAYAARIV SEVARGDLTV
QVKLRPGDQA SLLYAMKTMV DKLAAVLTEV SSGAQALASA SEEISATAQS LSQAASEQAA
GVEETSASVE QMTASIAQNT ENAKVTDSMA GQASLQAAEG GSAVKSTVEA MTQIAKKISI
IDDIAYQTNL LALNAAIEAA RAGEHGKGFA VVAAEVRKLA ERSQVAAQEI GEVAGSSVEL
AQKAGRLLDE MVPSIKKTSD LVQEITAASE EQSSGVAQIN SAIGQLSQTT QQNASSSEEL
AATAEEMSGQ AEQLQQAVSF FRVDGSERQA ARRAPAAAPR GRVFAPAKRA PAMEAAPDDS
NFVRF
//
