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Database: UniProt
Entry: A0A090IQ85_9BACI
LinkDB: A0A090IQ85_9BACI
Original site: A0A090IQ85_9BACI 
ID   A0A090IQ85_9BACI        Unreviewed;       565 AA.
AC   A0A090IQ85;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:CEE00226.1};
GN   ORFNames=BT1A1_0365 {ECO:0000313|EMBL:CEE00226.1};
OS   Caldibacillus thermoamylovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX   NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE00226.1, ECO:0000313|Proteomes:UP000040576};
RN   [1] {ECO:0000313|EMBL:CEE00226.1, ECO:0000313|Proteomes:UP000040576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg Daniel;
RL   Submitted (JUL-2014) 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; CCRF01000011; CEE00226.1; -; Genomic_DNA.
DR   RefSeq; WP_034767483.1; NZ_JAMAXM010000006.1.
DR   AlphaFoldDB; A0A090IQ85; -.
DR   Proteomes; UP000040576; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000040576};
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        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          207..260
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          279..515
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   565 AA;  62631 MW;  D695DDCB88CCF9E5 CRC64;
     MKHFFNFKTI NKKIIVGFTV VILISSLLVV YNLFSFYATN KKTEDIVDQQ LQFVIANDQL
     AYNVSERLAL VRGYILYGDN DYRKKFNQYT GESKNIQEQI LKIDKSKEVK DLFAKQENWE
     RVIVQDVYTE LSKGNEEQAL KTLSEKVEPL SDELVTAYST QSEKRQKEIN DMGDQIIHSG
     QTSMMISVII SIIVIISSII VAFFTGKSIS KPIKLVEERM NLIASGNLSG KPLETQLLDE
     TGHLIQSTNR MNLQMRELIS KIKSVSDTVT SQSEELTQSA NEVKAGAEQT AVTMQNLAAN
     AETQANRAER LSSIMKSFHE KVEAANDNGV RVEQTSKHIL EMSSEGGRLM SSSTAQMEKI
     DSIVKQTVEK VQGLDTESQK ISKLVSVIKE IADQTNLLAL NAAIEAARAG EHGKGFAVVA
     DEVRKLAEQV SFSVKDITGI VANIQNEVSE VTDVLEEGYT EVEQGTSQIK MTEERFKQIN
     LAITEMANHI KQISMNLAEI ANNSEEMSVS VHEIAATAQE AAAGIEQTSA SSQQTSSSME
     IITESSNLLA KLADEMNKLI GTFKL
//
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