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Database: UniProt
Entry: A0A1W9RT00_9BACT
LinkDB: A0A1W9RT00_9BACT
Original site: A0A1W9RT00_9BACT 
ID   A0A1W9RT00_9BACT        Unreviewed;       653 AA.
AC   A0A1W9RT00;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B6D55_02565 {ECO:0000313|EMBL:OQX87719.1};
OS   Candidatus Omnitrophica bacterium 4484_70.2.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1970783 {ECO:0000313|EMBL:OQX87719.1, ECO:0000313|Proteomes:UP000192395};
RN   [1] {ECO:0000313|Proteomes:UP000192395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) 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:OQX87719.1}.
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DR   EMBL; NATM01000013; OQX87719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9RT00; -.
DR   STRING; 1970783.B6D55_02565; -.
DR   Proteomes; UP000192395; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR029150; dCache_3.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
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; PF14827; dCache_3; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 1.
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   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..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          295..348
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          367..624
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   653 AA;  72311 MW;  F469E0D8E1873D31 CRC64;
     MWRSFKNKIG LLLVIVAIVP LLIIFFIFSK ELKQTLLRQK QRNIEKVQKY LKNTFEFKKK
     LIINYLNLLK EITGIRDAVT YTINTKDRKP LIEAILPYYK QIGLDTLQII KKDGEVLVRT
     DDVESIGESL KFQNVVKQAL EGKLSIGLEK ERGIYLLKGT VPLKTAEGIV GVICIGEFLD
     KEFAEEISQV TLTELAIFYK KKLIASSFSK KKIAEKKLYE IINRKVTGFF PINGKLYHFS
     PFTYSLGEAK SPLLIAIGIN AEPLINTERR MKFILVVLLG IIGTGSVFVG FFFSQGLVKP
     LLLLEKFAFN VASTSDLTQK IKIKSKDEIG RLASAFNKMI ESLSEVIKEV RKTTEKVNNF
     AKNSSASAQR VNVSTQQVST TIQQITQGAN VQVKKVEEAK EVIGKMVISI KQMTELATQG
     AQNSLRTQES AQKGMQTSSE AVEKIDKIIN TAMNVSGIVR KLDERSQEIS RIVETMSKIA
     DQTNLLALNA AIEAARAGEA GRGFAVVAEE VRKLAESSAQ AAVQVAKLIQ NIQKETEETV
     TSVEIAYKEV KGGKQVIGKV KEMLEKILKS AENTAQQVGE IAKSAEVQLA NAHKITQATE
     EITTIAEGNA SSVEEVSSSV EEVTASMEEL SSTSQELVSA TSKLENLLKK FKI
//
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