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Database: UniProt
Entry: A0A0Q6VMS2_9BURK
LinkDB: A0A0Q6VMS2_9BURK
Original site: A0A0Q6VMS2_9BURK 
ID   A0A0Q6VMS2_9BURK        Unreviewed;       455 AA.
AC   A0A0Q6VMS2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=PAS domain-containing protein {ECO:0000259|SMART:SM00091};
GN   ORFNames=ASD15_17075 {ECO:0000313|EMBL:KQV79748.1};
OS   Massilia sp. Root351.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV79748.1, ECO:0000313|Proteomes:UP000051876};
RN   [1] {ECO:0000313|EMBL:KQV79748.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV79748.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV79748.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV79748.1,
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:KQV79748.1}.
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DR   EMBL; LMDJ01000033; KQV79748.1; -; Genomic_DNA.
DR   RefSeq; WP_057157866.1; NZ_LMDJ01000033.1.
DR   AlphaFoldDB; A0A0Q6VMS2; -.
DR   OrthoDB; 8752517at2; -.
DR   Proteomes; UP000051876; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   Gene3D; 1.20.5.1930; -; 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; IPR036890; HATPase_C_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF10; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051876};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          47..113
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|SMART:SM00091"
FT   REGION          160..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  47826 MW;  2A855AB59067F87F CRC64;
     MSKGNHPRSD ALRQWQTLQL SKIELELQQQ ALSALQQRSE QARTGQALYQ QLFEQSPACT
     YALDQGGLVV CANQAGAALL AQSAAALQGQ PFERYLAPEQ QPRWRAFTAI LRSGDGRAGM
     ETQLFAGIPG ACAVRIDACL DAASGLCCLV IAPLAAAPSA QPDSGAAGHR EQAFPGHEPL
     AAGPLGARLA AQLAQQGALA MASQVAAQVA ERTTALTLDN TQLRLLAEHE ANALEAARLD
     MARAMHDNVG QNLLALRIEA ALLDQRTRRH GGPLHQRASA ALENVDTTLR SVRAILNQLR
     PAVLDLGLHA AVDWLLADFR KRSGLVCTLD VPDEQAFDCL ESGAALMLFR QLQALLASVQ
     RDGGASAVAV SLRRLGRSGA VLLVTDDGAG DTAVDSDAGG GVALAGRRQR QALAMLAIGE
     RLRAHGGVLE VDYGAAQGCR VSMRLPGQVG QAGNS
//
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