ID A0A3N5BV88_9THEO Unreviewed; 570 AA.
AC A0A3N5BV88;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:RPF49815.1};
GN ORFNames=EDD75_0639 {ECO:0000313|EMBL:RPF49815.1};
OS Thermodesulfitimonas autotrophica.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermodesulfitimonas.
OX NCBI_TaxID=1894989 {ECO:0000313|EMBL:RPF49815.1, ECO:0000313|Proteomes:UP000282654};
RN [1] {ECO:0000313|EMBL:RPF49815.1, ECO:0000313|Proteomes:UP000282654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102936 {ECO:0000313|EMBL:RPF49815.1,
RC ECO:0000313|Proteomes:UP000282654};
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 (NOV-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:RPF49815.1}.
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DR EMBL; RKRE01000001; RPF49815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5BV88; -.
DR Proteomes; UP000282654; 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; IPR004089; MCPsignal_dom.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF17202; sCache_3_3; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 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:UP000282654};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..307
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 305..541
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 570 AA; 60116 MW; FB782029CE7EDF9A CRC64;
MLLNEKESKE MFPGVLGKGV IAGAGLWVKI AFLFSVANPW AFEGGIPVRV YSLRKAMAFL
VAVTVVFAAA ACTLAVVLVA RASLTAQLQG YLKRDLAGTY DILFEHHYPG DWRVAGDKLY
KGKVLMNGNF AVVDQVKEDF GTEATIFMGD TRVATTVKDA TGHRKVGTKA APYVVEAVLK
QGQNYYGTAD VAGTPHLTAY MPLKDAQGKV VGMWFVGVPL TEVKAATGRM VWSAFLVGLA
VLGILLLVFV PVIQRILTPI RIVAERIEKV ADGDLAAVNL GAQRFRALRM LADATGRMVG
QLRELAIRVQ GAAVEVSGKS ENLAASAEEL SATVQTVAAT VEELSAGAEE TAAHAQTAAE
IADRMEREAN EGIQALGGAV SGIRNAQEAV DKGAGLVREL GERSAAIGQI TEVIKGIAEQ
TNLLALNAAI EAARAGEHGR GFAVVAEEVR KLAEQSAQAA EEISKIIAEI QRGTGEVVAA
IDRASTTVHQ GAGAVIETEE RLKSILKGVA DTLAGIRDIA RATEQASQGT QNVAQSVQEA
SRVAEQVGQM ASELAQQAAE LQGALKVFKL
//
