ID A0A366HGM5_9BURK Unreviewed; 584 AA.
AC A0A366HGM5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:RBP40672.1};
GN ORFNames=DFR37_10310 {ECO:0000313|EMBL:RBP40672.1};
OS Eoetvoesiella caeni.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Eoetvoesiella.
OX NCBI_TaxID=645616 {ECO:0000313|EMBL:RBP40672.1, ECO:0000313|Proteomes:UP000253628};
RN [1] {ECO:0000313|EMBL:RBP40672.1, ECO:0000313|Proteomes:UP000253628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25520 {ECO:0000313|EMBL:RBP40672.1,
RC ECO:0000313|Proteomes:UP000253628};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RBP40672.1}.
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DR EMBL; QNRQ01000003; RBP40672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366HGM5; -.
DR OrthoDB; 9806477at2; -.
DR Proteomes; UP000253628; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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: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; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 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.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000253628};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..271
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 276..505
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 528..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 60960 MW; DBE89823BCAF36F7 CRC64;
MNWFTDMKIG VKLIGGFLLV AIIAAIIGVM GLRAVDQLHS LAARMYDVEL VGLRHATDAK
AAVLMAGRTA RSALLAPTAA ERDQQLEALK QYLSAADTEL KTLDTLLVTQ EGKTFVRNTH
DALRAYEGGI KKMIGVLVAE PPGQAVKANE ILTHEIHLTG NKLEDLMDGL VQGKQNNAKQ
AAVQTNGIYD FIFAVMISLT AGGALLALGL GVLITRGLTR QLGGEPKEVA GVAHAIADGD
LTTAIDTAKA RDGSVIHAMS RMQASLRQVV GSVRESSDSI ATGSHQIALG NADLSQRTEE
QAANITETAA AMEQLASTVK SNAEVSEQAV TLATTASTVA SQGGHAVNNV VETMDGIAQA
SRKIVDIIAV IDGIAFQTNI LALNASVEAA RAGEEGRGFA VVASEVRNLA QKSAAAAKEI
KTLIDDSASR VEAGSQMADA AGATMLDIVN QVKRVTDLIN EIHSATTEQA SGLEQINNAV
TQLSDVTQQN AALVEESAAA AESLDAQAEQ LVAAVGAFKL GQRRAGRPEN ASALNANRAS
APTVRQQASG PAMHRLGSVA AASRLRSPLV ETPLAAKNDE WESF
//
