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Database: UniProt
Entry: A0A1G5DKJ8_9FIRM
LinkDB: A0A1G5DKJ8_9FIRM
Original site: A0A1G5DKJ8_9FIRM 
ID   A0A1G5DKJ8_9FIRM        Unreviewed;       560 AA.
AC   A0A1G5DKJ8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SCY15176.1};
GN   ORFNames=SAMN05660668_01600 {ECO:0000313|EMBL:SCY15176.1};
OS   Pseudobutyrivibrio sp. AR14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=1520804 {ECO:0000313|EMBL:SCY15176.1, ECO:0000313|Proteomes:UP000198746};
RN   [1] {ECO:0000313|EMBL:SCY15176.1, ECO:0000313|Proteomes:UP000198746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR14 {ECO:0000313|EMBL:SCY15176.1,
RC   ECO:0000313|Proteomes:UP000198746};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; FMUY01000007; SCY15176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5DKJ8; -.
DR   Proteomes; UP000198746; 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; cd06225; HAMP; 1.
DR   Gene3D; 6.10.340.10; -; 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   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 1.
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   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        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          212..264
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          314..543
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   560 AA;  60456 MW;  4CBF67E4E0D0DDA0 CRC64;
     MKNNRNAKGT IAGALREFSG FTIRMFLANA IIMIVFFVII FINVYNFYNV QFVTEKYQME
     IRKDVQTINK RLLFAVASND PEVTADQKAD LEKRFPKIEG YFGTISANLN NAELGANLDT
     YWKGFEDASF EMLALVEAGE TDKAVEYFNS TLNEAAETLA DALDETGELA ESAAAGKYMT
     IMVVVVVAAI VLVIALVIII LINRKRSADM IKGIERDLDI LAKASEEIAQ GNVHVEIDYE
     ADNEIGRVAK QLKIAVESLV YYIDEIAAVM STMAGGNFNI NFERDFDGDF KEIQTAVETF
     SKEISESMTE IMEVSDMVSD GANQIAGAGQ NLADTVTSQA NIVDDLSVTV KDITEQISNN
     SSDATAISQE VEVVAQNIVE GNQKMQDVVN AMDAISASSQ EISKIIDTIN AIADQTNLLS
     LNASIEAARA GEAGKGFAVV ATEVSQLAGQ TVEAAQNTAG LINASLKSVE EGITIANETA
     EKLNGMVAQV QGIAEKVKTI ADESSSQATS VKEMSSNISE ISSVGQNNAA TSQESLALSY
     EMNEHANSLK GLVEKFELKK
//
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