ID A0A103EHV8_9BURK Unreviewed; 714 AA.
AC A0A103EHV8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KVE35130.1};
GN ORFNames=WS68_08445 {ECO:0000313|EMBL:KVE35130.1};
OS Burkholderia sp. TSV86.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1385594 {ECO:0000313|EMBL:KVE35130.1, ECO:0000313|Proteomes:UP000066043};
RN [1] {ECO:0000313|EMBL:KVE35130.1, ECO:0000313|Proteomes:UP000066043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV86 {ECO:0000313|EMBL:KVE35130.1,
RC ECO:0000313|Proteomes:UP000066043};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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:KVE35130.1}.
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DR EMBL; LOWB01000078; KVE35130.1; -; Genomic_DNA.
DR RefSeq; WP_059571529.1; NZ_LOWB01000078.1.
DR AlphaFoldDB; A0A103EHV8; -.
DR Proteomes; UP000066043; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd11386; MCP_signal; 1.
DR CDD; cd19407; Tar_Tsr_sensor; 1.
DR Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR035440; 4HB_MCP_dom_sf.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..267
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 272..501
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 523..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..517
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 678..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 72278 MW; FBB7936212E8DB5C CRC64;
MLDNWSIRTT LTAIGTMMVL VAALVGGLGL YALHEAGGSL DAIAHGDLPT IHTLDEASSY
LLRARVSLGR FKALTESGNA DEAQKVLARA QELYAKSAQH WQTYLAASKD GIDPALTDEL
AARYGALVKD GVEPEFAAAR AGDLAAYRAI AETKISPMFV AYDNAASAVA AAHASRAEGR
FGATQARISL MTTLIAAGIA LAFAIVIGTR FALRGLIVEP LAVAAAQFER IATGDLAPVE
RAHGTNEIGR LFEGIGRMRA AVSQMVAAVH RGVAAIDAGA HEIASGNADL SQRTESQAAS
LQETASSMEQ LTGTVRQNAE NARQASQLAV NASDIATQGG EVVGQVVVTM QDIAASSTKV
ADIIGTIEGI AFQTNILALN AAVEAARAGE QGRGFAVVAG EVRSLAQRSA GAAKEIKQLI
GDSALKVQSG SALVERAGAT MAEIVQAVRR VTDIMGEISA ASEEQSTGIV QVTRAVSQMD
AVTQQNAALV EQAAAAAASL EEQMRQLKQV VAGWRIDGVI ASGSTGSTGE KAARAREAAG
GPFVADRADR AGAAGMRAAA GLRPPSVSAA QGAPHAASVS AAAAASSATA ALAASQAMPA
SARAAQHGSS ASTAAAMSAA GSPTRPASDA AHASPAARAA FAKTSEAAPK FASPASAYAP
KLAKPASAAR APQRASAAQP AETASASALK RPVLSNESQP ALASASSDDD WETF
//