ID B1KYL1_CLOBM Unreviewed; 572 AA.
AC B1KYL1;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ACA55004.1};
GN OrderedLocusNames=CLK_2180 {ECO:0000313|EMBL:ACA55004.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA55004.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA55004.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP000962; ACA55004.1; -; Genomic_DNA.
DR RefSeq; WP_012343037.1; NC_010520.1.
DR AlphaFoldDB; B1KYL1; -.
DR KEGG; cbl:CLK_2180; -.
DR HOGENOM; CLU_000445_107_19_9; -.
DR Proteomes; UP000000722; Chromosome.
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 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; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00672; HAMP; 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 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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 285..456
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 572 AA; 64819 MW; 49B19FAF15A28449 CRC64;
MLDKVKIKVK MLILTIIMLI SILIVGVLGV FNIWKNNRDI NSLYEKNLIS VKVLDDNRNQ
SRALEADILY IILNQDNKEE QSKRIEDIKI REKKFNDNFK TLQSTKLDEQ EIKFMDQMSR
HLNEYSIRRN IVVKMALAGK YKEAYEEFYS LNRTIESFHN RLRDLANYNE KKAESINSEN
NKQYKMTILL FLAITILTIL IGPIFTLNIA KSIAKPMENL ANNLNLLSEG DFTENITDEY
LNRSDEIGIV FTSLKKMHSN IKEMIFKVKD EIEKSMEFNA AISILFNELN KNIEEVSSTT
EQLSAGMEET AASSEEMNST SNQIERVIES VTEQAKEVSD RSVTINKRAQ DLKIGAENSR
KNTLNVYEMN KGKLSKAIED TKSVDEINKL LEAILDITDQ TNLLALNAAI EAARAGEAGK
GFAVVAEEVR KLAEESSNTA GQIQRITETV VSSVKELANN SQQLLDFMNV NIVKDYDDFV
WTGDSYSNDA KYYNKVSLDL SDNCKNILVS INNITEVING VALSAEEGAV GATSIAEKTN
IIVENTDLVK EKSEQSKERA ELLMELVNKF RI
//
