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Database: UniProt
Entry: A0A1H9A0L4_9FIRM
LinkDB: A0A1H9A0L4_9FIRM
Original site: A0A1H9A0L4_9FIRM 
ID   A0A1H9A0L4_9FIRM        Unreviewed;       596 AA.
AC   A0A1H9A0L4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SEP69538.1};
GN   ORFNames=SAMN02910382_00724 {ECO:0000313|EMBL:SEP69538.1};
OS   Butyrivibrio sp. TB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1520809 {ECO:0000313|EMBL:SEP69538.1, ECO:0000313|Proteomes:UP000198682};
RN   [1] {ECO:0000313|EMBL:SEP69538.1, ECO:0000313|Proteomes:UP000198682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TB {ECO:0000313|EMBL:SEP69538.1,
RC   ECO:0000313|Proteomes:UP000198682};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; FOER01000004; SEP69538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9A0L4; -.
DR   Proteomes; UP000198682; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
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; PF17200; sCache_2; 1.
DR   SMART; SM01049; Cache_2; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          233..288
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          307..564
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          343..370
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   596 AA;  64053 MW;  AB10C11A994C2940 CRC64;
     MKNLKVRTKL SILLAVVVIA MIGLSGMAII GMSQIQSTSV EIIKDSISQD YDDQIKNEVD
     TAFAICDTYY GLYQAGAMTL DEAKEYSATV IRGITYGEAG YLWVDTYDGV NVVLLGNETE
     GTNRLGSKDS QGFAMVADFI EGAKKNLNEG YFNEYYFPKA GETEPSPKRA YTKAYPNFEW
     VIGTGNYIDY IDSTTAEHEG VLSAKAANIS VISIGTGVVL IIISVVLTVM LTRSIVGPLK
     DTSVWLDEMG SGDFSRHIDP KYTELHDDFG ILMQQLEKMR HSVSKLLKGA KNDSISVHDS
     SIELAQGAAQ TKDNSANITI AVGEIADGAT NQAESVQDGV NAIQEILQNV ETLNNEVDAA
     DEKANAMAES SDNMQANFEK LKVAMTQSAD SLADVSEKVK AMGDSVEEVQ NAVAAINEIS
     SRTNLLSLNA SIEAARAGEA GKGFAVVATE IQDLSVQSSQ SAQRIGEIMK GLSDSSESAV
     RTVNQLNDAV GGQQQISDET AEAVRDVISM IADVRENFNK AKDAAEITRT KCVDLNDTMS
     SLSAISEENA ASAQETSASM QEVNNTVENI SDLSATLENI STELTELLEV FHVSDL
//
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