ID A0A0K0G9B0_9FIRM Unreviewed; 572 AA.
AC A0A0K0G9B0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=WH51_10710 {ECO:0000313|EMBL:KKE78769.1};
OS Bacilli bacterium VT-13-104.
OC Bacteria; Bacillota; Bacilli.
OX NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE78769.1, ECO:0000313|Proteomes:UP000034981};
RN [1] {ECO:0000313|Proteomes:UP000034981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA Tetz V., Tetz G.;
RT "Bacilli bacterium VT-13-104.";
RL Submitted (APR-2015) 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:KKE78769.1}.
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DR EMBL; LAZH01000042; KKE78769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0G9B0; -.
DR PATRIC; fig|1637974.4.peg.2262; -.
DR OrthoDB; 107771at2; -.
DR Proteomes; UP000034981; 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; 1.10.8.500; HAMP domain in histidine kinase; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000034981};
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 191..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..267
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 286..543
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 83..110
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 572 AA; 62976 MW; 803F42BF53524E5A CRC64;
MRKSEREKNK FFSINKKIVL SFLVIGIVFF SASAIYFTQL KAVEKSNLEI MNRHVAILEH
IDEIQIQAKS QIDLLRAFFL SGNADLVAEM EEANQNVQEM INTSRELVNT QDEKDSLRKI
EIMNKLFLDA ATVAIPYQDS NSPVKLISSL ADIPSIMATK MVDESKILAE STNKEIEVAI
HDNKEKVQQT FILLIISAVV SLGLLVVIGM AVSRLIVKPI VQVSNMAREI ANGNLRGEKI
EIKINDEIGD LSSSFNLMRD NLHQVLYKVE QNAEQLAATS EELTASTEQT SQASEQISDA
IQEIAVGAEN QADSTQNATT VVKEMSASMD QASSSMGMVA RLTSKTSEKA ADGQQVVNYT
TRQMEQIQQK VSQTYEIVQV LSEKSNEVGE ITTIIAKISE QTNLLALNAA IESVRAGEHG
KGFAVVAEEV RKLANQSGEA TAHIREIIEE IQNETRKVVD SMQEGKESTD QGIKLVNQTG
DTFKEITSMV EDVAEQSVHV SNIIEEVNNG SQSMVELVET ISTVSDQASA NSQNVAAASE
EQTASMEEIS ASSQMLRQMA TDLQDLVQTF RF
//
