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Database: UniProt
Entry: A0A1M5T621_9CLOT
LinkDB: A0A1M5T621_9CLOT
Original site: A0A1M5T621_9CLOT 
ID   A0A1M5T621_9CLOT        Unreviewed;       546 AA.
AC   A0A1M5T621;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer with TarH sensor {ECO:0000313|EMBL:SHH46174.1};
GN   ORFNames=SAMN02745207_01220 {ECO:0000313|EMBL:SHH46174.1};
OS   Clostridium grantii DSM 8605.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121316 {ECO:0000313|EMBL:SHH46174.1, ECO:0000313|Proteomes:UP000184447};
RN   [1] {ECO:0000313|EMBL:SHH46174.1, ECO:0000313|Proteomes:UP000184447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8605 {ECO:0000313|EMBL:SHH46174.1,
RC   ECO:0000313|Proteomes:UP000184447};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQXM01000005; SHH46174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5T621; -.
DR   STRING; 1121316.SAMN02745207_01220; -.
DR   Proteomes; UP000184447; 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   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:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 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   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184447};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          239..291
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          296..525
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          353..380
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   546 AA;  60405 MW;  5C18E24EEE85A8F1 CRC64;
     MKTLTYLKRK FKKKESRRGG ILKKTNFITG FKNIKLAKQL ISCFALIGIL TSFVGIIALK
     NMNNTNESSI EIYEKRLLPI TYVTGVQKNM LLIRAKHLYM LSEKDTAKIS EAVDEIEELK
     VGYQELITKY KETDLTKAEE NYLIELQSSL TSYNQFAMMY EMKLKENKYE EAMSYVVSFN
     EAWDKVSENI EHLIQINKEE AALLLDNNQT YFEASYFRMI LTILVVLSAA IVLGMWVAGL
     ISKPINKLLS ASTQIAEGNL DIEIDIQNKS EIGVLSTAFN KMTYNINHAL YNINESAEQV
     ASGANQVANS SMLLSQGATE QASAIEQLSS TVEEISKQTK YNATNANLAK NITEKAKVNA
     EESKKQMNEM LNAMSEINES SMNISKVIKV IEEIAFQTNI LALNAAIEAA RAGQYGKGFS
     VVAEEVRNLA LRSSNAAKET TDMIEGSVKK VEVGSKIANL TSNELNNIVQ DVSKAAKLVG
     DIALASNEQA IGADQVNRSI NQITKVVQTT SSTSEETASA SEELSGQAAI LKEQVGNFKL
     KNNKSE
//
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